1. 1H-Purin-6-amine flavin dinucleotide
2. 1H-Purin-6-amine flavine dinucleotide
3. Adenine-flavin dinucleotide
4. Adenine-flavine dinucleotide
5. Adenine-riboflavin dinuceotide
6. Adenine-riboflavin dinucleotide
7. Adenine-riboflavine dinucleotide
8. FAD
9. Flamitajin B
10. Flanin F
11. Flavin adenine dinucleotide
12. Flavin-adenine dinucleotide
13. Flavine adenosine diphosphate
14. Flavine-adenine dinucleotide
15. Flavitan
16. Flaziren
17. Isoalloxazine-adenine dinucleotide
18. Riboflavin 5'-adenosine diphosphate
19. Riboflavin-adenine dinucleotide
20. Riboflavine-adenine dinucleotide
21. flavin adenine dinucleotide oxidized

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• Cytoplasm
• endoplasmic reticulum
• mitochondria
• peroxisome

• Blood

• 606788 (Anorexia nervosa)

1. Flatz G, Simmersbach F: Flavin adenine dinucleotide concentration in erythrocytes with normal and deficient glucose-6-phosphate dehydrogenase. Klin Wochenschr. 1970 Sep 1;48(17):1071-2. [PubMed ]
2. Zempleni J: Determination of riboflavin and flavocoenzymes in human blood plasma by high-performance liquid chromatography. Ann Nutr Metab. 1995;39(4):224-6. [PubMed ]
3. Becker K, Wilkinson AR: Flavin adenine dinucleotide levels in erythrocytes of very low birthweight infants under vitamin supplementation. Biol Neonate. 1993;63(2):80-5. [PubMed ]
4. Lisowsky T, Lee JE, Polimeno L, Francavilla A, Hofhaus G: Mammalian augmenter of liver regeneration protein is a sulfhydryl oxidase. Dig Liver Dis. 2001 Mar;33(2):173-80. [PubMed ]
5. Cimino JA, Jhangiani S, Schwartz E, Cooperman JM: Riboflavin metabolism in the hypothyroid human adult. Proc Soc Exp Biol Med. 1987 Feb;184(2):151-3. [PubMed ]
6. Kodentsova VM, Vrzhesinskaia OA, Alekseeva IA, Spirichev VB: [Comparison of biochemical criteria for supplying the human body with riboflavin] Vopr Med Khim. 1991 Sep-Oct;37(5):76-9. [PubMed ]
7. Lopez-Anaya A, Mayersohn M: Quantification of riboflavin, riboflavin 5'-phosphate and flavin adenine dinucleotide in plasma and urine by high-performance liquid chromatography. J Chromatogr. 1987 Dec 25;423:105-13. [PubMed ]
8. Van Binsbergen CJ, Odink J, Van den Berg H, Koppeschaar H, Coelingh Bennink HJ: Nutritional status in anorexia nervosa: clinical chemistry, vitamins, iron and zinc. Eur J Clin Nutr. 1988 Nov;42(11):929-37. [PubMed ]
9. Mohrenweiser HW, Novotny JE: ACP1GUA-1--a low-activity variant of human erythrocyte acid phosphatase: association with increased glutathione reductase activity. Am J Hum Genet. 1982 May;34(3):425-33. [PubMed ]
10. Gianazza E, Vergani L, Wait R, Brizio C, Brambilla D, Begum S, Giancaspero TA, Conserva F, Eberini I, Bufano D, Angelini C, Pegoraro E, Tramontano A, Barile M: Coordinated and reversible reduction of enzymes involved in terminal oxidative metabolism in skeletal muscle mitochondria from a riboflavin-responsive, multiple acyl-CoA dehydrogenase deficiency patient. Electrophoresis. 2006 Mar;27(5-6):1182-98. [PubMed ]
11. Cimino JA, Noto RA, Fusco CL, Cooperman JM: Riboflavin metabolism in the hypothyroid newborn. Am J Clin Nutr. 1988 Mar;47(3):481-3. [PubMed ]
12. Wikipedia

1. Dihydrolipoyl dehydrogenase, mitochondrial precursor
2. Long-chain specific acyl-CoA dehydrogenase, mitochondrial precursor
3. Short-chain specific acyl-CoA dehydrogenase, mitochondrial precursor
4. Medium-chain specific acyl-CoA dehydrogenase, mitochondrial precursor
5. NADH-ubiquinone oxidoreductase chain 1
6. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
7. NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial precursor
8. Peroxisomal sarcosine oxidase
9. Peroxisomal N1-acetyl-spermine/spermidine oxidase
10. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12
11. NADH-cytochrome b5 reductase 3
12. Aldehyde oxidase
13. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1
14. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2
15. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3
16. NADH-ubiquinone oxidoreductase chain 4L
17. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
18. Thioredoxin reductase 1, cytoplasmic precursor
19. Lathosterol oxidase
20. NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial precursor
21. Ribosyldihydronicotinamide dehydrogenase [quinone]
22. NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
23. NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial precursor
24. Dimethylaniline monooxygenase [N-oxide-forming] 5
25. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial precursor
26. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6
27. Acyl-coenzyme A oxidase 1, peroxisomal
28. D-aspartate oxidase
29. NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4
30. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial precursor
31. NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial precursor
32. Squalene monooxygenase
33. NADH-ubiquinone oxidoreductase chain 2
34. Dimethylaniline monooxygenase [N-oxide-forming] 2
35. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
36. Thioredoxin reductase 2, mitochondrial precursor
37. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
38. Methionine synthase
39. Amine oxidase [flavin-containing] B
40. NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial precursor
41. NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial precursor
42. Acyl-coenzyme A oxidase 2, peroxisomal
43. Dimethylaniline monooxygenase [N-oxide-forming] 4
44. Isovaleryl-CoA dehydrogenase, mitochondrial precursor
45. Amine oxidase [flavin-containing] A
46. NADH dehydrogenase [ubiquinone] 1 subunit C2
47. Dimethylaniline monooxygenase [N-oxide-forming] 3
48. NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3
49. NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
50. Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial precursor
51. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial precursor
52. NADH-ubiquinone oxidoreductase chain 4
53. Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial precursor
54. NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial precursor
55. Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase
56. NADPH--cytochrome P450 reductase
57. Dihydroorotate dehydrogenase, mitochondrial precursor
58. Dimethylaniline monooxygenase [N-oxide-forming] 1
59. NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor
60. Methylenetetrahydrofolate reductase
61. NADH-ubiquinone oxidoreductase chain 6
62. NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13
63. NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial precursor
64. Acyl-coenzyme A oxidase 3, peroxisomal
65. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
66. Glutathione reductase, mitochondrial precursor
67. Glycerol-3-phosphate dehydrogenase, mitochondrial precursor
68. Heme oxygenase 1
69. Retinal dehydrogenase 1
70. Choline dehydrogenase, mitochondrial precursor
71. Glutaryl-CoA dehydrogenase, mitochondrial precursor
72. Dimethylglycine dehydrogenase, mitochondrial precursor
73. NADPH:adrenodoxin oxidoreductase, mitochondrial precursor
74. Retinal dehydrogenase 2
75. D-amino-acid oxidase
76. Methionine synthase reductase, mitochondrial precursor
77. tRNA-dihydrouridine synthase 2-like
78. Dihydropyrimidine dehydrogenase [NADP+] precursor
79. Sarcosine dehydrogenase, mitochondrial precursor
80. Nitric oxide synthase, inducible
81. Nitric-oxide synthase, brain
82. Nitric-oxide synthase, endothelial
83. Protoporphyrinogen oxidase
84. NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial precursor
85. Alkyldihydroxyacetonephosphate synthase, peroxisomal precursor
86. Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial precursor
87. NAD(P)H dehydrogenase [quinone] 1
88. Cytochrome b-245 heavy chain
89. Electron transfer flavoprotein subunit alpha, mitochondrial precursor
90. Putative dimethylaniline monooxygenase [N-oxide-forming] 6
91. 24-dehydrocholesterol reductase precursor
92. Amyloid beta A4 protein precursor
93. Electron transfer flavoprotein subunit beta
94. Proline oxidase, mitochondrial precursor
95. D-2-hydroxyglutarate dehydrogenase, mitochondrial precursor
96. L-2-hydroxyglutarate dehydrogenase, mitochondrial precursor
97. Kynurenine 3-monooxygenase
98. Spermine oxidase
99. Apoptosis-inducing factor 1, mitochondrial precursor
100. Cryptochrome-1
101. Dual oxidase 2 precursor
102. OTTHUMP00000017001
103. Probable D-lactate dehydrogenase, mitochondrial precursor
104. Isobutyryl-CoA dehydrogenase, mitochondrial precursor
105. Acyl-CoA dehydrogenase family member 9, mitochondrial precursor
106. Probable proline dehydrogenase 2
107. Dual oxidase 1 precursor
108. Thioredoxin reductase 3
109. NADH-cytochrome b5 reductase 1
110. NADH-cytochrome b5 reductase 2
111. Cytochrome b5 reductase 4
112. Probable NADH-cytochrome b5 reductase FLJ00377
113. Putative uncharacterized protein DKFZp686B0215
114. cDNA FLJ76840, highly similar to Homo sapiens succinate dehydrogenase complex, subunit A, flavoprotein
115. cDNA FLJ76015, highly similar to Homo sapiens glutaryl-Coenzyme A dehydrogenase
116. Acyl-Coenzyme A dehydrogenase, long chain
117. cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
118. FAD synthetase
119. Ubiquinone biosynthesis monooxygenase COQ6
120. NADPH oxidase 5
121. NADPH oxidase 3
122. Metalloreductase STEAP3
123. Very long-chain specific acyl-CoA dehydrogenase, mitochondrial precursor
124. Acyl-coenzyme A oxidase-like protein
125. Apoptosis-inducing factor 2
126. Apoptosis-inducing factor 3
127. FAD-linked sulfhydryl oxidase ALR
128. Flavin-containing amine oxidase domain-containing protein 1
129. Cryptochrome-2
130. tRNA-dihydrouridine synthase 1-like
131. tRNA-dihydrouridine synthase 3-like
132. tRNA-dihydrouridine synthase 4-like
133. ERO1-like protein alpha precursor
134. ERO1-like protein beta precursor
135. FAD-dependent oxidoreductase domain-containing protein 1
136. FAD-dependent oxidoreductase domain-containing protein 2
137. Lysine-specific histone demethylase 1
138. NEDD9-interacting protein with calponin homology and LIM domains
139. Protein MICAL-2
140. Protein MICAL-3
141. Protein MTO1 homolog, mitochondrial precursor
142. NADPH-dependent FMN and FAD containing oxidoreductase
143. NADPH oxidase homolog 1
144. NADPH oxidase 4
145. L-amino-acid oxidase precursor
146. Oxidoreductase NAD-binding domain-containing protein 1 precursor
147. Prenylcysteine oxidase 1 precursor
148. Prenylcysteine oxidase-like precursor
149. [Pyruvate dehydrogenase [lipoamide]]-phosphatase 2, mitochondrial precursor
150. Pyridine nucleotide-disulphide oxidoreductase domain 1
151. Sulfhydryl oxidase 1 precursor
152. Sulfhydryl oxidase 2 precursor
153. Renalase precursor
154. All-trans-retinol 13,14-reductase precursor
155. Sulfide:quinone oxidoreductase, mitochondrial precursor
156. Metalloreductase STEAP1
157. Metalloreductase STEAP2
158. Metalloreductase STEAP4
159. Succinate dehydrogenase complex, subunit C delta5 alternative splicing variant
160. Integral membrane protein CII-3b (Succinate dehydrogenase complex, subunit C, integral membrane protein, 15kDa, isoform CRA_g) (Succinate dehydrogenase complex, subunit C delta3 alternative splicing variant)
161. cDNA FLJ77934, highly similar to Homo sapiens flavin containing monooxygenase 1 (FMO1), mRNA (Flavin containing monooxygenase 1, isoform CRA_a)
162. Flavin containing monooxygenase 2
163. Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c)
164. NADH dehydrogenase (Ubiquinone) 1 alpha subcomplex, 4, 9kDa (NADH dehydrogenase (Ubiquinone) 1 alpha subcomplex, 4, 9kDa, isoform CRA_b)
165. NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 1, 7kDa (NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 1, 7kDa, isoform CRA_b)
166. NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 2, 8kDa (NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 2, 8kDa, isoform CRA_a)
167. cDNA FLJ76517, highly similar to Homo sapiens NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 6, 17kDa (NDUFB6), nuclear gene encoding mitochondrial protein, transcript variant 1, mRNA (NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 6, 17kDa, isofo
168. cDNA FLJ76373, highly similar to Homo sapiens NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 8, 19kDa (NDUFB8), mRNA (NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 8, 19kDa, isoform CRA_b)
169. cDNA FLJ78612, highly similar to Homo sapiens NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 10, 22kDa (NDUFB10), mRNA (NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 10, 22kDa, isoform CRA_b)
170. cDNA FLJ76555, highly similar to Homo sapiens NADH dehydrogenase (ubiquinone) 1, subcomplex unknown, 1, 6kDa (NDUFC1), mRNA (Putative uncharacterized protein NDUFC1)
171. cDNA FLJ76512, highly similar to Homo sapiens NADH dehydrogenase (ubiquinone) flavoprotein 3, 10kDa (NDUFV3), transcript variant 2, mRNA (NADH dehydrogenase (Ubiquinone) flavoprotein 3, 10kDa, isoform CRA_b)
172. Peroxisomal N1-acetyl-spermine/spermidine oxidase (PAO) (Polyamine oxidase (Exo-N4-amino), isoform CRA_a)
173. cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
174. cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c)
175. cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
176. cDNA, FLJ92337, highly similar to Homo sapiens succinate dehydrogenase complex, subunit B, iron sulfur (Ip) (SDHB), mRNA (Succinate dehydrogenase complex, subunit B, iron sulfur (Ip), isoform CRA_a)
177. Putative uncharacterized protein
178. cDNA, FLJ92690, Homo sapiens NAD(P)H dehydrogenase, quinone 1 (NQO1), mRNA (NAD(P)H dehydrogenase, quinone 1, isoform CRA_c)
179. cDNA, FLJ93696, highly similar to Homo sapiens flavin containing monooxygenase 3 (FMO3), mRNA (Flavin containing monooxygenase 3, isoform CRA_b)
180. cDNA, FLJ96516, Homo sapiens NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 5,13kDa (NDUFA5), nuclear gene encoding mitochondrial protein, mRNA (NADH dehydrogenase (Ubiquinone) 1 alpha subcomplex, 5, 13kDa, isoform CRA_b)
181. NADH dehydrogenase (Ubiquinone) 1 alpha subcomplex, 8, 19kDa (cDNA, FLJ94833, Homo sapiens NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 8, 19kDa (NDUFA8), mRNA)
182. cDNA, FLJ92143, Homo sapiens NADH dehydrogenase (ubiquinone) 1, alpha/betasubcomplex, 1, 8kDa (NDUFAB1), mRNA (NADH dehydrogenase (Ubiquinone) 1, alpha/beta subcomplex, 1, 8kDa, isoform CRA_b)
183. cDNA, FLJ93971, Homo sapiens NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 9,22kDa (NDUFB9), mRNA (NADH dehydrogenase (Ubiquinone) 1 beta subcomplex, 9, 22kDa)
184. cDNA, FLJ94420, Homo sapiens NADH dehydrogenase (ubiquinone) Fe-S protein 3, 30kDa(NADH-coenzyme Q reductase) (NDUFS3), mRNA (NADH dehydrogenase (Ubiquinone) Fe-S protein 3, 30kDa (NADH-coenzyme Q reductase), isoform CRA_a)
185. Cytochrome b5 reductase 1, isoform CRA_b

1. Dihydrolipoamide dehydrogenase
2. Glycine cleavage system L protein

MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGTDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF

• Citrate Cycle (map00020 )
• Gluconeogenesis (map00010 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Pyruvate Metabolism (map00620 )

• protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+

• Pyr_redox (PF00070 )
• Pyr_redox_2 (PF07992 )
• Pyr_redox_dim (PF02852 )

• None

• None

ATGCAGAGCTGGAGTCGTGTGTACTGCTCCTTGGCCAAGAGAGGCCATTTCAATCGAATA
TCTCATGGCCTACAGGGACTTTCTGCAGTGCCTCTGAGAACTTACGCAGATCAGCCGATT
GATGCTGATGTAACAGTTATAGGTTCTGGTCCTGGAGGATATGTTGCTGCTATTAAAGCT
GCCCAGTTAGGCTTCAAGACAGTCTGCATTGAGAAAAATGAAACACTTGGTGGAACATGC
TTGAATGTTGGTTGTATTCCTTCTAAGGCTTTATTGAACAACTCTCATTATTACCATATG
GCCCATGGAACAGATTTTGCATCTAGAGGAATTGAAATGTCCGAAGTTCGCTTGAATTTA
GACAAGATGATGGAGCAGAAGAGTACTGCAGTAAAAGCTTTAACAGGTGGAATTGCCCAC
TTATTCAAACAGAATAAGGTTGTTCATGTCAATGGATATGGAAAGATAACTGGCAAAAAT
CAAGTCACTGCTACGAAAGCTGATGGCGGCACTCAGGTTATTGATACAAAGAACATTCTT
ATAGCCACGGGTTCAGAAGTTACTCCTTTTCCTGGAATCACGATAGATGAAGATACAATA
GTGTCATCTACAGGTGCTTTATCTTTAAAAAAAGTTCCAGAAAAGATGGTTGTTATTGGT
GCAGGAGTAATAGGTGTAGAATTGGGTTCAGTTTGGCAAAGACTTGGTGCAGATGTGACA
GCAGTTGAATTTTTAGGTCATGTAGGTGGAGTTGGAATTGATATGGAGATATCTAAAAAC
TTTCAACGCATCCTTCAAAAACAGGGGTTTAAATTTAAATTGAATACAAAGGTTACTGGT
GCTACCAAGAAGTCAGATGGAAAAATTGATGTTTCTATTGAAGCTGCTTCTGGTGGTAAA
GCTGAAGTTATCACTTGTGATGTACTCTTGGTTTGCATTGGCCGACGACCCTTTACTAAG
AATTTGGGACTAGAAGAGCTGGGAATTGAACTAGATCCTAGAGGTAGAATTCCAGTCAAT
ACCAGATTTCAAACTAAAATTCCAAATATCTATGCCATTGGTGATGTAGTTGCTGGTCCA
ATGCTGGCTCACAAAGCAGAGGATGAAGGCATTATCTGTGTTGAAGGAATGGCTGGTGGT
GCTGTGCACATTGACTACAATTGTGTGCCATCAGTGATTTACACACACCCTGAAGTTGCT
TGGGTTGGCAAATCAGAAGAGCAGTTGAAAGAAGAGGGTATTGAGTACAAAGTTGGGAAA
TTCCCATTTGCTGCTAACAGCAGAGCTAAGACAAATGCTGACACAGATGGCATGGTGAAG
ATCCTTGGGCAGAAATCGACAGACAGAGTACTGGGAGCACATATTCTTGGACCAGGTGCT
GGAGAAATGGTAAATGAAGCTGCTCTTGCTTTGGAATATGGAGCATCCTGTGAAGATATA
GCTAGAGTCTGTCATGCACATCCGACCTTATCAGAAGCTTTTAGAGAAGCAAATCTTGCT
GCGTCATTTGGCAAATCAATCAACTTTTGA

1. Otulakowski G, Robinson BH: Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. J Biol Chem. 1987 Dec 25;262(36):17313-8. [PubMed ]
2. Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS: Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1422-6. [PubMed ]
3. Feigenbaum AS, Robinson BH: The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics. 1993 Aug;17(2):376-81. [PubMed ]
4. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
5. Johanning GL, Morris JI, Madhusudhan KT, Samols D, Patel MS: Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10964-8. [PubMed ]
6. Liu TC, Kim H, Arizmendi C, Kitano A, Patel MS: Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5186-90. [PubMed ]
7. Hong YS, Kerr DS, Craigen WJ, Tan J, Pan Y, Lusk M, Patel MS: Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency. Hum Mol Genet. 1996 Dec;5(12):1925-30. [PubMed ]
8. Shaag A, Saada A, Berger I, Mandel H, Joseph A, Feigenbaum A, Elpeleg ON: Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews. Am J Med Genet. 1999 Jan 15;82(2):177-82. [PubMed ]

1. LCAD

MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SATEFMFEETRNYVKQRKAFGKTVAHLQTVQHQLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK

• Fatty Acid Metabolism (map00071 )

• acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor

• Acyl-CoA_dh_1 (PF00441 )
• Acyl-CoA_dh_M (PF02770 )
• Acyl-CoA_dh_N (PF02771 )

• None

• None

ATGGCCGCACGCCTTCTCCGAGGGTCCCTACGCGTCCTGGGCGGCCACCGTGCGCCGCGC
CAGCTGCCCGCCGCGCGATGTTCTCATTCCGGAGGGGAAGAACGTCTAGAAACTCCTTCT
GCTAAAAAATTAACAGATATAGGAATTCGAAGAATCTTTTCTCCAGAGCATGACATTTTC
CGGAAAAGTGTAAGGAAGTTTTTCCAAGAAGAAGTGATTCCTCATCACTCAGAATGGGAG
AAAGCTGGAGAAGTAAGTAGGGAGGTTTGGGAAAAAGCTGGAAAACAAGGACTGCTTGGT
GTCAATATTGCAGAGCATCTTGGTGGAATTGGAGGGGATCTGTACTCCGCAGCTATTGTC
TGGGAGGAGCAAGCTTATTCAAATTGTTCAGGCCCAGGTTTTAGTATTCATTCAGGTATT
GTCATGTCCTATATTACAAACCATGGCTCAGAAGAACAGATTAAGCACTTTATTCCCCAG
ATGACTGCAGGCAAATGTATTGGTGCAATAGCAATGACAGAGCCTGGAGCTGGAAGTGAC
TTACAGGGAATAAAAACAAATGCTAAAAAGGATGGAAGTGACTGGATTCTCAATGGAAGC
AAGGTGTTCATCAGTAATGGGTCATTAAGTGATGTTGTGATTGTAGTTGCGGTCACAAAT
CATGAAGCTCCCTCCCCTGCCCATGGTATTAGCCTTTTTCTGGTGGAAAATGGAATGAAA
GGATTTATCAAGGGACGAAAGCTACATAAAATGGGATTAAAAGCCCAGGATACCGCAGAA
CTATTCTTTGAAGATATACGGTTGCCAGCTAGTGCCCTACTTGGAGAAGAGAATAAAGGC
TTCTATTACATCATGAAAGAGCTTCCACAGGAAAGGCTGTTAATTGCTGATGTGGCAATT
TCAGCTAGTGAATTCATGTTTGAAGAAACCAGGAACTATGTTAAACAAAGAAAAGCTTTT
GGCAAAACAGTTGCTCACCTACAGACAGTGCAACATAAATTAGCAGAATTAAAAACACAT
ATATGTGTAACCCGAGCATTTGTGGACAACTGTCTCCAGCTGCATGAAGCGAAACGTTTG
GACTCCGCCACTGCTTGCATGGCGAAATATTGGGCATCTGAGTTACAAAATAGTGTAGCT
TACGACTGTGTACAGCTCCATGGAGGTTGGGGATACATGTGGGAGTACCCAATTGCAAAA
GCTTATGTGGATGCCAGAGTTCAGCCAATCTATGGTGGTACAAATGAAATAATGAAGGAG
CTGATTGCAAGAGAGATTGTCTTTGACAAGTAG

1. Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1991 Nov;11(3):609-20. [PubMed ]
2. Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1992 Mar;12(3):626. [PubMed ]

1. SCAD
2. Butyryl-CoA dehydrogenase

MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQV
DKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN
SLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLN
GTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTAN
LIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF
GAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS

• Butyrate Metabolism (map00650 )
• Fatty Acid Metabolism (map00071 )
• Valine, Leucine and Isoleucine Degradation (map00280 )

• butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor

• Acyl-CoA_dh_1 (PF00441 )
• Acyl-CoA_dh_M (PF02770 )
• Acyl-CoA_dh_N (PF02771 )

• None

• None

ATGGCCGCCGCGCTGCTCGCCCGGGCCTCGGGCCCTGCCCGCAGAGCTCTCTGTCCTAGG
GCCTGGCGGCAGTTACACACCATCTACCAGTCTGTGGAACTGCCCGAGACACACCAGATG
TTGCTCCAGACATGCCGGGACTTTGCCGAGAAGGAGTTGTTTCCCATTGCAGCCCAGGTG
GATAAGGAACATCTCTTCCCAGCGGCTCAGGTGAAGAAGATGGGCGGGCTTGGGCTTCTG
GCCATGGACGTGCCCGAGGAGCTTGGCGGTGCTGGCCTCGATTACCTGGCCTACGCCATC
GCCATGGAGGAGATCAGCCGTGGCTGCGCCTCCACCGGAGTCATCATGAGTGTCAACAAC
TCTCTCTACCTGGGGCCCATCTTGAAGTTTGGCTCCAAGGAGCAGAAGCAGGCGTGGGTC
ACGCCTTTCACCAGTGGTGACAAAATTGGCTGCTTTGCCCTCAGCGAACCAGGGAACGGC
AGTGATGCAGGAGCTGCGTCCACCACCGCCCGGGCCGAGGGCGACTCATGGGTTCTGAAT
GGAACCAAAGCCTGGATCACCAATGCCTGGGAGGCTTCGGCTGCCGTGGTCTTTGCCAGC
ACGGACAGAGCCCTGCAAAACAAGGGCATCAGTGCCTTCCTGGTCCCCATGCCAACGCCT
GGGCTCACGTTGGGGAAGAAAGAAGACAAGCTGGGCATCCGGGGCTCATCCACGGCCAAC
CTCATCTTTGAGGACTGTCGCATCCCCAAGGACAGCATCCTGGGGGAGCCAGGGATGGGC
TTCAAGATAGCCATGCAAACCCTGGACATGGGCCGCATCGGCATCGCCTCCCAGGCCCTG
GGCATTGCCCAGACCGCCCTCGATTGTGCTGTGAACTACGCTGAGAATCGCATGGCCTTC
GGGGCGCCCCTCACCAAGCTCCAGGTCATCCAGTTCAAGTTGGCAGACATGGCCCTGGCC
CTGGAGAGTGCCCGGCTGCTGACCTGGCGCGCTGCCATGCTGAAGGATAACAAGAAGCCT
TTCATCAAGGAGGCAGCCATGGCCAAGCTGGCCGCCTCGGAGGCCGCGACCGCCATCAGC
CACCAGGCCATCCAGATCCTGGGCGGCATGGGCTACGTGACAGAGATGCCGGCAGAGCGG
CACTACCGCGACGCCCGCATCACTGAGATCTACGAGGGCACCAGCGAAATCCAGCGGCTG
GTGATCGCCGGGCATCTGCTCAGGAGCTACCGGAGCTGA

1. Naito E, Ozasa H, Ikeda Y, Tanaka K: Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1989 May;83(5):1605-13. [PubMed ]
2. Corydon MJ, Andresen BS, Bross P, Kjeldsen M, Andreasen PH, Eiberg H, Kolvraa S, Gregersen N: Structural organization of the human short-chain acyl-CoA dehydrogenase gene. Mamm Genome. 1997 Dec;8(12):922-6. [PubMed ]
3. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed ]
4. Naito E, Indo Y, Tanaka K: Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1990 May;85(5):1575-82. [PubMed ]
5. Gregersen N, Winter VS, Corydon MJ, Corydon TJ, Rinaldo P, Ribes A, Martinez G, Bennett MJ, Vianey-Saban C, Bhala A, Hale DE, Lehnert W, Kmoch S, Roig M, Riudor E, Eiberg H, Andresen BS, Bross P, Bolund LA, Kolvraa S: Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria. Hum Mol Genet. 1998 Apr;7(4):619-27. [PubMed ]
6. Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N: Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. [PubMed ]

1. MCAD

MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEI
IPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ
TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKG
DEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNM
GQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEAT
KYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF
AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK
N

• Beta Alanine Metabolism (map00410 )
• Fatty Acid Metabolism (map00071 )
• Propanoate Metabolism (map00640 )
• Valine, Leucine and Isoleucine Degradation (map00280 )

• acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor

• Acyl-CoA_dh_1 (PF00441 )
• Acyl-CoA_dh_M (PF02770 )
• Acyl-CoA_dh_N (PF02771 )

• None

• None

ATGGCAGCGGGGTTCGGGCGATGCTGCAGGGTCCTGAGAAGTATTTCTCGTTTTCATTGG
AGATCACAGCATACAAAAGCCAATCGACAACGTGAACCAGGATTAGGATTTAGTTTTGAG
TTCACCGAACAGCAGAAAGAATTTCAAGCTACTGCTCGTAAATTTGCCAGAGAGGAAATC
ATCCCAGTGGCTGCAGAATATGATAAAACTGGTGAATATCCAGTCCCCCTAATTAGAAGA
GCCTGGGAACTTGGTTTAATGAACACACACATTCCAGAGAACTGTGGAGGTCTTGGACTT
GGAACTTTTGATGCTTGTTTAATTAGTGAAGAATTGGCTTATGGATGTACAGGGGTTCAG
ACTGCTATTGAAGGAAATTCTTTGGGGCAAATGCCTATTATTATTGCTGGAAATGATCAA
CAAAAGAAGAAGTATTTGGGGAGAATGACTGAGGAGCCATTGATGTGTGCTTATTGTGTA
ACAGAACCTGGAGCAGGCTCTGATGTAGCTGGTATAAAGACCAAAGCAGAAAAGAAAGGA
GATGAGTATATTATTAATGGTCAGAAGATGTGGATAACCAACGGAGGAAAAGCTAATTGG
TATTTTTTATTGGCACGTTCTGATCCAGATCCTAAAGCTCCTGCTAATAAAGCCTTTACT
GGATTCATTGTGGAAGCAGATACCCCAGGAATTCAGATTGGGAGAAAGGAATTAAACATG
GGCCAGCGATGTTCAGATACTAGAGGAATTGTCTTCGAAGATGTGAAAGTGCCTAAAGAA
AATGTTTTAATTGGTGACGGAGCTGGTTTCAAAGTTGCAATGGGAGCTTTTGATAAAACC
AGACCTGTAGTAGCTGCTGGTGCTGTTGGATTAGCACAAAGAGCTTTGGATGAAGCTACC
AAGTATGCCCTGGAAAGGAAAACTTTCGGAAAGCTACTTGTAGAGCACCAAGCAATATCA
TTTATGCTGGCTGAAATGGCAATGAAAGTTGAACTAGCTAGAATGAGTTACCAGAGAGCA
GCTTGGGAGGTTGATTCTGGTCGTCGAAATACCTATTATGCTTCTATTGCAAAGGCATTT
GCTGGAGATATTGCAAATCAGTTAGCTACTGATGCTGTGCAGATACTTGGAGGCAATGGA
TTTAATACAGAATATCCTGTAGAAAAACTAATGAGGGATGCCAAAATCTATCAGATTTAT
GAAGGTACTTCACAAATTCAAAGACTTATTGTAGCCCGTGAACACATTGACAAGTACAAA
AATTAA

1. Kelly DP, Kim JJ, Billadello JJ, Hainline BE, Chu TW, Strauss AW: Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4068-72. [PubMed ]
2. Matsubara Y, Narisawa K, Miyabayashi S, Tada K, Coates PM, Bachmann C, Elsas LJ 2nd, Pollitt RJ, Rhead WJ, Roe CR: Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Biochem Biophys Res Commun. 1990 Aug 31;171(1):498-505. [PubMed ]
3. Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Biochemistry. 1996 Sep 24;35(38):12412-20. [PubMed ]
4. Tanaka K, Yokota I, Coates PM, Strauss AW, Kelly DP, Zhang Z, Gregersen N, Andresen BS, Matsubara Y, Curtis D, et al.: Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene. Hum Mutat. 1992;1(4):271-9. [PubMed ]
5. Yokota I, Indo Y, Coates PM, Tanaka K: Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. J Clin Invest. 1990 Sep;86(3):1000-3. [PubMed ]
6. Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW: Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9236-40. [PubMed ]
7. Yokota I, Coates PM, Hale DE, Rinaldo P, Tanaka K: Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. Am J Hum Genet. 1991 Dec;49(6):1280-91. [PubMed ]
8. Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al.: Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. Hum Genet. 1991 Apr;86(6):545-51. [PubMed ]
9. Blakemore AI, Singleton H, Pollitt RJ, Engel PC, Kolvraa S, Gregersen N, Curtis D: Frequency of the G985 MCAD mutation in the general population. Lancet. 1991 Feb 2;337(8736):298-9. [PubMed ]
10. Andresen BS, Jensen TG, Bross P, Knudsen I, Winter V, Kolvraa S, Bolund L, Ding JH, Chen YT, Van Hove JL, et al.: Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. Am J Hum Genet. 1994 Jun;54(6):975-88. [PubMed ]
11. Ziadeh R, Hoffman EP, Finegold DN, Hoop RC, Brackett JC, Strauss AW, Naylor EW: Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. Pediatr Res. 1995 May;37(5):675-8. [PubMed ]
12. Brackett JC, Sims HF, Steiner RD, Nunge M, Zimmerman EM, deMartinville B, Rinaldo P, Slaugh R, Strauss AW: A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. J Clin Invest. 1994 Oct;94(4):1477-83. [PubMed ]
13. Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, Yokota I, Hart K, Packman S, Harpey JP, Saudubray JM, Hale DE, Bolund L, Kolvraa S, Gregersen N: The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet. 1997 May;6(5):695-707. [PubMed ]
14. Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S: Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site. Biochem J. 1999 Jan 15;337 ( Pt 2):225-30. [PubMed ]
15. Yang BZ, Ding JH, Zhou C, Dimachkie MM, Sweetman L, Dasouki MJ, Wilkinson J, Roe CR: Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Mol Genet Metab. 2000 Mar;69(3):259-62. [PubMed ]
16. Andresen BS, Dobrowolski SF, O'Reilly L, Muenzer J, McCandless SE, Frazier DM, Udvari S, Bross P, Knudsen I, Banas R, Chace DH, Engel P, Naylor EW, Gregersen N: Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency. Am J Hum Genet. 2001 Jun;68(6):1408-18. Epub 2001 May 8. [PubMed ]
17. Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E: Molecular and functional characterisation of mild MCAD deficiency. Hum Genet. 2001 May;108(5):404-8. [PubMed ]
18. Albers S, Levy HL, Irons M, Strauss AW, Marsden D: Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis. 2001 Jun;24(3):417-8. [PubMed ]

1. NADH dehydrogenase subunit 1

MPMANLLLLIVPILIAMAFLMLTERKILGYMQLRKGPNVVGPYGLLQPFADAMKLFTKEP
LKPATSTITLYITAPTLALTIALLLWTPLPMPNPLVNLNLGLLFILATSSLAVYSILWSG
WASNSNYALIGALRAVAQTISYEVTLAIILLSTLLMSGSFNLSTLITTQEHLWLLLPSWP
LAMMWFISTLAETNRTPFDLAEGESELVSGFNIEYAAGPFALFFMAEYTNIIMMNTLTTT
IFLGTTYDALSPELYTTYFVTKTLLLTSLFLWIRTAYPRFRYDQLMHLLWKNFLPLTLAL
LMWYVSMPITISSIPPQT

• Oxidative phosphorylation (map00190 )
• Ubiquinone Biosynthesis (map00130 )

• NADH + H+ + ubiquinone = NAD+ + ubiquinol

• NADHdh (PF00146 )

• 1-18

• 68-90
• 100-122
• 135-157
• 172-191
• 222-244
• 254-273
• 293-315

1. Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
2. Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
3. Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
4. Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
5. Sanger F, Coulson AR, Barrell BG, Smith AJ, Roe BA: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161-78. [PubMed ]
6. Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
7. Howell N, Bindoff LA, McCullough DA, Kubacka I, Poulton J, Mackey D, Taylor L, Turnbull DM: Leber hereditary optic neuropathy: identification of the same mitochondrial ND1 mutation in six pedigrees. Am J Hum Genet. 1991 Nov;49(5):939-50. [PubMed ]
8. Huoponen K, Vilkki J, Aula P, Nikoskelainen EK, Savontaus ML: A new mtDNA mutation associated with Leber hereditary optic neuroretinopathy. Am J Hum Genet. 1991 Jun;48(6):1147-53. [PubMed ]
9. Howell N, Kubacka I, Xu M, McCullough DA: Leber hereditary optic neuropathy: involvement of the mitochondrial ND1 gene and evidence for an intragenic suppressor mutation. Am J Hum Genet. 1991 May;48(5):935-42. [PubMed ]
10. Johns DR, Berman J: Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1324-30. [PubMed ]
11. Majander A, Huoponen K, Savontaus ML, Nikoskelainen E, Wikstrom M: Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 1991 Nov 4;292(1-2):289-92. [PubMed ]
12. Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
13. Johns DR, Neufeld MJ, Park RD: An ND-6 mitochondrial DNA mutation associated with Leber hereditary optic neuropathy. Biochem Biophys Res Commun. 1992 Sep 30;187(3):1551-7. [PubMed ]
14. Shoffner JM, Brown MD, Torroni A, Lott MT, Cabell MF, Mirra SS, Beal MF, Yang CC, Gearing M, Salvo R, et al.: Mitochondrial DNA variants observed in Alzheimer disease and Parkinson disease patients. Genomics. 1993 Jul;17(1):171-84. [PubMed ]
15. Jaksch M, Hofmann S, Kaufhold P, Obermaier-Kusser B, Zierz S, Gerbitz KD: A novel combination of mitochondrial tRNA and ND1 gene mutations in a syndrome with MELAS, cardiomyopathy, and diabetes mellitus. Hum Mutat. 1996;7(4):358-60. [PubMed ]
16. Nakagawa Y, Ikegami H, Yamato E, Takekawa K, Fujisawa T, Hamada Y, Ueda H, Uchigata Y, Miki T, Kumahara Y, et al.: A new mitochondrial DNA mutation associated with non-insulin-dependent diabetes mellitus. Biochem Biophys Res Commun. 1995 Apr 17;209(2):664-8. [PubMed ]

1. E- NPP 1
2. Phosphodiesterase I/nucleotide pyrophosphatase 1
3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
4. NPPase]

MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED

• Nicotinate and Nicotinamide Metabolism (map00760 )
• Pantothenate and CoA Biosynthesis (map00770 )
• Purine Metabolism (map00230 )
• Riboflavin Metabolism (map00740 )
• Starch and Sucrose Metabolism (map00500 )

• A dinucleotide + H2O = 2 mononucleotides

• Phosphodiest (PF01663 )
• Somatomedin_B (PF01033 )

• None

• 77-97

ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA

1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed ]
2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed ]
3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed ]
5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed ]
6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed ]
7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed ]

1. NADH-ubiquinone oxidoreductase 49 kDa subunit
2. Complex I-49kD
3. CI-49kD

MAALRALCGFRGVAAQVLRPGAGVRLPIQPSRGVRQWQPDVEWAQQFGGAVMYPSKETAH
WKPPPWNDVDPPKDTIVKNITLNFGPQHPAAHGVLRLVMELSGEMVRKCDPHIGLLHRGT
EKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSLAVEKLLNIRPPPRAQWIRVLFGEITRL
LNHIMAVTTHALDLGAMTPFFWLFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGL
MDDIYQFSKNFSLRLDELEELLTNNRIWRNRTIDIGVVTAEEALNYGFSGVMLRGSGIQW
DLRKTQPYDVYDQVEFDVPVGSRGDCYDRYLCRVEEMRQSLRIIAQCLNKMPPGEIKVDD
AKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPY
RCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEVDR

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• Complex1_49kDa (PF00346 )

• 1-15

ATGGCGGCGCTGAGGGCTTTGTGCGGCTTCCGGGGCGTCGCGGCCCAGGTGCTGCGGCCT
GGGGCTGGAGGCCGATTGCCGATTCAGCCCAGCAGAGGTGTTCGGCAGTGGCAGCCAGAT
GTGGAATGGGCACAGCAGTTTGGGGGAGCTGTTATGTACCCAAGCAAAGAAACAGCCCAC
TGGAAGCCTCCACCTTGGAATGATGTGGACCCTCCAAAGGACACAATTGTGAAGAACATT
ACCCTGAACTTTGGGCCCCAACACCCAGCAGCGCATGGTGTCCTGCGACTAGTGATGGAA
TTGAGTGGGGAGATGGTGCGGAAGTGTGATCCTCACATCGGGCTCCTGCACCGAGGCACT
GAGAAGCTCATTGAATACAAGACCTATCTTCAGGCCCTTCCATACTTTGACCGGCTAGAC
TATGTGTCCATGATGTGTAACGAACAGGCCTATTCTCTAGCTGTGGAGAAGTTGCTAAAC
ATCCGGCCTCCTCCTCGGGCACAGTGGATCCGAGTGCTGTTTGGAGAAATCACACGTTTG
TTGAACCACATCATGGCTGTGACCACACATGCCCTGGACCTTGGGGCCATGACCCCTTTC
TTCTGGCTGTTTGAAGAAAGGGAGAAGATGTTTGAGTTCTACGAGCGAGTGTCTGGAGCC
CGAATGCATGCTGCTTATATCCGGCCAGGAGGAGTGCACCAGGACCTACCCCTTGGGCTT
ATGGATGACATTTATCAGTTTTCTAAGAACTTCTCTCTTCGGCTTGATGAGTTGGAGGAG
TTGCTGACCAACAATAGGATCTGGCGAAATCGGACAATTGACATTGGGGTTGTAACAGCA
GAAGAAGCACTTAACTATGGTTTTAGTGGAGTGATGCTTCGGGGCTCAGGCATCCAGTGG
GACCTGCGGAAGACCCAGCCCTATGATGTTTACGACCAGGTTGAGTTTGATGTTCCTGTT
GGTTCTCGAGGGGACTGCTATGATAGGTACCTGTGCCGGGTGGAGGAGATGCGCCAGTCC
CTGAGAATTATCGCACAGTGTCTAAACAAGATGCCTCCTGGGGAGATCAAGGTTGATGAT
GCCAAAGTGTCTCCACCTAAGCGAGCAGAGATGAAGACTTCCATGGAGTCACTGATTCAT
CACTTTAAGTTGTATACTGAGGGCTACCAAGTTCCTCCAGGAGCCACATATACTGCCATT
GAGGCTCCCAAGGGAGAGTTTGGGGTGTACCTGGTGTCTGATGGCAGCAGCCGCCCTTAT
CGATGCAAGATCAAGGCTCCTGGTTTTGCCCATCTGGCTGGTTTGGACAAGATGTCTAAG
GGACACATGTTGGCAGATGTCGTTGCCATCATAGGTACCCAAGATATTGTATTTGGAGAA
GTAGATCGGTGA

1. Procaccio V, de Sury R, Martinez P, Depetris D, Rabilloud T, Soularue P, Lunardi J, Issartel J: Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory Complex I and immunodetection of the mature protein in mitochondria. Mamm Genome. 1998 Jun;9(6):482-4. [PubMed ]
2. Loeffen J, van den Heuvel L, Smeets R, Triepels R, Sengers R, Trijbels F, Smeitink J: cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed. Biochem Biophys Res Commun. 1998 Jun 29;247(3):751-8. [PubMed ]

1. PSO
2. L-pipecolate oxidase
3. L-pipecolic acid oxidase

MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL

• Lysine Degradation (map00310 )

• L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2

• DAO (PF01266 )

• None

• 7-26

ATGGCGGCTCAGAAAGATCTCTGGGACGCCATTGTGATTGGGGCGGGGATCCAGGGCTGC
TTCACTGCATACCACCTCGCCAAACACAGGAAGAGGATCCTCCTGCTGGAGCAGTTCTTT
CTACCACACTCCCGAGGAAGCTCCCATGGACAAAGCCGGATAATCCGAAAGGCGTACCTG
GAAGACTTTTACACCCGGATGATGCATGAGTGCTATCAGATATGGGCCCAGCTGGAGCAC
GAGGCTGGAACCCAATTGCACAGGCAGACTGGATTACTGCTGCTGGGAATGAAAGAGAAT
CAAGAATTAAAGACAATCCAGGCCAATCTGTCGAGGCAGAGGGTAGAACACCAGTGTCTT
TCATCTGAGGAACTGAAGCAACGTTTCCCAAATATTCGGTTGCCCAGGGGAGAAGTGGGG
CTCTTGGACAATTCCGGAGGAGTTATCTATGCATATAAGGCCCTCAGAGCCCTGCAGGAT
GCAATTCGACAGCTAGGAGGCATAGTGCGTGACGGAGAGAAGGTGGTGGAGATAAACCCA
GGGCTACTGGTCACGGTGAAAACCACCTCCAGGAGCTACCAAGCTAAGAGCTTGGTCATC
ACAGCAGGTCCTTGGACCAACCAGCTCCTCCGTCCCCTGGGCATTGAGATGCCTCTCCAG
ACCCTGCGGATCAACGTGTGTTACTGGCGAGAGATGGTTCCTGGGAGCTATGGTGTGTCC
CAGGCCTTTCCGTGCTTCCTGTGGCTGGGCTTGTGTCCCCACCACATCTACGGACTGCCC
ACAGGAGAGTACCCAGGGCTGATGAAGGTCAGCTATCACCACGGCAACCACGCAGACCCT
GAGGAGCGGGACTGCCCCACAGCACGCACAGACATCGGAGACGTCCAGATCCTGAGCAGC
TTTGTCAGAGATCACTTACCTGATCTGAAGCCCGAGCCTGCTGTCATTGAGAGCTGCATG
TACACGAATACCCCTGATGAGCAGTTCATTCTCGATCGCCACCCAAAGTATGACAACATT
GTCATTGGTGCTGGATTCTCTGGGCACGGGTTCAAGCTGGCCCCTGTGGTGGGGAAGATC
CTGTATGAATTAAGCATGAAATTAACACCATCTTATGACTTGGCACCTTTTCGAATCAGC
CGTTTCCCAAGCCTGGCCAAAGCCCACCTGTGA

1. Dodt G, Kim DG, Reimann SA, Reuber BE, McCabe K, Gould SJ, Mihalik SJ: L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases. Biochem J. 2000 Feb 1;345 Pt 3:487-94. [PubMed ]
2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

1. Polyamine oxidase

MESTGSVGEAPGGPRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCF
GGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLVETGGHVGLPSVSYASSGT
SVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKEIGQHVARLCGHSAFPHLR
VLEATARAGGRIRSERCFGGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLV
ETGGHVGLPSVSYASSGASVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKE
IGQHVAGWTEDEETRKLKLAVLNSFFNLECCVSGTHSMDLVALAPFGEYTVLPGLDCTFS
KGYQGLTNCMMAALPEDTVVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAHH
VIVTVPLGFLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFLEFEEPFWEPDCQLIQLV
WEDTSPLEDAAPELQDAWFRKLIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLC
LTQVLRRVTGNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAG
AQLQILFAGEATHRTFYSTTHGALLSGWREADRLLSLWAPQVQQPRPRL

• N1-acetylspermine + O2 + H2O = N1-acetylspermidine + 3-aminopropanal + H2O2

• Amino_oxidase (PF01593 )

• None

• None

GGTGGCGTGGTGGAGGTAGGTGCTCACTGGATCCATGGGCCCTCCCAGGGTAACCCCGTC
TTCCAGCTGGCTGTTGAGTACGGGCTGCTGGGGGAGAAGGAGCTGTCCCAGGAGAACCAG
CTGGTGGAGACCGGGGGTCACGTGGGCCTGCCCTCCGTGAGCTACGCCAGCTCCGGGGCC
AGCGTGAGCCTCCAGCTGGTGGCGGAGATGGCGACTCTGTTCTACGGCCTGATAGACCAG
ACCCGGGAGTTCCTGCACGCTGCAGAGACCCCGGTGCCCAGCGTCGGGGAGTACCTCAAG
AAGGAGATTGGCCAGCACGTGGCCGGCTGGACAGAGGATGAGGAGACCAGGAAGCTGAAG
CTGGCCGTCCTGAACTCCTTCTTCAACCTGGAATGCTGTGTGAGCGGCACCCACAGCATG
GACCTGGTGGCCCTGGCACCCTTTGGGGAGTATACCGTGCTGCCGGGGCTGGACTGCACC
TTTTCTAAGGGCTATCAAGGACTCACAAACTGCATGATGGCCGCCCTGCCGGAGGACACT
GTAGTTTTTGAGAAGCCTGTGAAGACCATCCACTGGAACGGGTCCTTCCAGGAGGCAGCC
TTTCCCGGGGAGACCTTTCCAGTGTCGGTAGAGTGTGAGGATGGAGACCGGTTCCCGGCG
CACCATGTCATCGTCACCGTGCCCTTAGGTTTTCTTAGGGAACATTTGGACACCTTCTTT
GACCCTCCCCTGCCGGCTGAGAAGGCAGAAGCAATCAGGAAGATAGGCTTTGGGACCAAC
AACAAAATCTTCCTGGAGTTTGAGGAGCCCTTCTGGGAGCCAGACTGCCAGCTGATCCAG
CTGGTGTGGGAGGACACGTCGCCCCTGGAGGATGCTGCCCCTGAGCTACAGGACGCCTGG
TTCCGGAAGCTCATTGGCTTTGGGGTCCTGCCTGCCTTTGCGTCTGTCCACGTTCTCTGT
GGGTTCATTGCCGGACTTGAGTCTGAGTTCATGGAGACTCTGTCGGATGAAGAAGTACTT
CTGTGTCTCACCCAAGTGCTCCGGAGAGTGACAGGAAACCCACGGCTCCCCGCGCCCAAG
AGCGTCCTGCGGTCTCGCTGGCACAGCGCCCCGTACACTAGGGGGTCCTACAGCTACGTG
GCCGTGGGCAGTACTGGGGGCGACCTGGACCTGCTGGCTCAGCCCCTCCCTGCAGACGGC
GCCGGCGCCCAGCTCCAGATCCTGTTTGCGGGGGAAGCCACACATCGCACGTTTTACTCC
ACGACGCACGGGGCTCTGCTGTCGGGATGGAGGGAGGCCGACCGCCTCCTCAGTCTGTGG
GCCCCGCAGGTGCAGCAGCCCAGGCCGAGGCTCTAG

1. Wu T, Yankovskaya V, McIntire WS: Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. J Biol Chem. 2003 Jun 6;278(23):20514-25. Epub 2003 Mar 26. [PubMed ]
2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

1. NADH-ubiquinone oxidoreductase subunit B17.2
2. Complex I-B17.2
3. CI-B17.2
4. CIB17.2
5. 13 kDa differentiation- associated protein

MELVQVLKRGLQQITGHGGLRGYLRVFFRTNDAKVGTLVGEDKYGNKYYEDNKQFFGRHR
WVVYTTEMNGKNTFWDVDGSMVPPEWHRWLHSMTDDPPTTKPLTARKFIWTNHKFNVTGT
PEQYVPYSTTRKKIQEWIPPSTPYK

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• NDUFA12 (PF05071 )

• None

• None

ATGGAGTTAGTGCAGGTCCTGAAACGCGGGCTGCAGCAGATCACCGGCCACGGCGGTCTC
CGAGGCTATCTACGGGTTTTTTTCAGGACAAATGATGCGAAGGTTGGTACATTAGTGGGG
GAAGACAAATATGGAAACAAATACTATGAAGACAACAAGCAATTTTTTGGCCGTCACCGA
TGGGTTGTATATACTACTGAAATGAATGGCAAAAACACATTCTGGGATGTGGATGGAAGC
ATGGTGCCTCCTGAATGGCATCGTTGGCTTCACAGTATGACTGATGATCCTCCAACAACA
AAACCACTTACTGCTCGTAAATTCATTTGGACGAACCATAAATTCAACGTGACTGGCACC
CCAGAACAATATGTACCTTATTCTACCACTAGAAAGAAGATTCAGGAGTGGATCCCACCT
TCAACACCTTACAAGTAA

1. Triepels R, Smeitink J, Loeffen J, Smeets R, Trijbels F, van den Heuvel L: Characterization of the human complex I NDUFB7 and 17.2-kDa cDNAs and mutational analysis of 19 genes of the HP fraction in complex I-deficient-patients. Hum Genet. 2000 Apr;106(4):385-91. [PubMed ]
2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

1. Cytochrome b5 reductase
2. B5R
3. Diaphorase-1[Contains: NADH-cytochrome b5 reductase 3 membrane-bound form
4. NADH-cytochrome b5 reductase 3 soluble form]

MGAQLSTLGHMVLFPVWFLYSLLMKLFQRSTPAITLESPDIKYPLRLIDREIISHDTRRF
RFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYFKDTHPK
FPAGGKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKFAIRPDKKSNPIIRTVKSVGMIAG
GTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLD
RAPEAWDYGQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDHVGHPTERCFV
F

• Aminosugars metabolism (map00530 )

• NADH + H+ + 2 ferricytochrome b5 = NAD+ + 2 ferrocytochrome b5

• FAD_binding_6 (PF00970 )
• NAD_binding_1 (PF00175 )

• 1-33

ATGGGGGCCCAGCTCAGCACGTTGGGCCATATGGTCCTCTTCCCAGTCTGGTTCCTGTAC
AGTCTGCTCATGAAGCTGTTCCAGGGCTCCACGCCAGCCATCACCCTCGAGAGCCCGGAC
ATCAAGTACCCGCTGCGGCTCATCGACCGGGAGATCATCAGCCATGACACCCGGCGCTTC
CGCTTTGCCCTGCCGCCACCCCAGCACATCCTGGGCCTCCCTGTCGGCCAGCACATCTAC
CTCTCGGCTCGAATTGATGGAAACCTGGTCGTCCGGCCCTATACACCAATCTCCAGCGAT
GATGACAAGGGCTTCGTGGACCTGGTCATCAAGGTTTACTTCAAGGACACCCATCCCAAG
TTTCCCGCTGGAGGGAAGATGTCTCAGTACCTGGAGAGCATGCAGATTGGAGACACCATT
GAGTTCCGGGGCCCCAGTGGGCTGCTGGTCTACCAGGGCAAAGGGAAGTTCGCCATCCGA
CCTGACAAAAAGTCCAACCCTATCATCAGGACAGTGAAGTCTGTGGGCATGATCGCGGGA
GGGACAGGCATCACCCCGATGCTGCAGGTGATCCGCGCCATCATGAAGGACCCTGATGAC
CACACTGTGTGCCACCTGCTCTTTGCCAACCAGACCGAGAAGGACATCCTGCTGCGACCT
GAGCTGGAGGAACTCAGGAACAAACATTCTGCACGCTTCAAGCTCTGGTACACGCTGGAC
AGAGCCCCTGAAGCCTGGGACTACGGCCAGGGCTTCGTGAATGAGGAGATGATCCGGGAC
CACCTTCCACCCCCAGAGGAGGAGCCGCTGGTGCTGATGTGTGGCCCCCCACCCATGATC
CAGTACGCCTGCCTTCCCAACCTGGACCACGTGGGCCACCCCACGGAGCGCTGCTTCGTC
TTCTGA

1. Tomatsu S, Kobayashi Y, Fukumaki Y, Yubisui T, Orii T, Sakaki Y: The organization and the complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene. Gene. 1989 Aug 15;80(2):353-61. [PubMed ]
2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
3. Yubisui T, Naitoh Y, Zenno S, Tamura M, Takeshita M, Sakaki Y: Molecular cloning of cDNAs of human liver and placenta NADH-cytochrome b5 reductase. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3609-13. [PubMed ]
4. Murakami K, Yubisui T, Takeshita M, Miyata T: The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases. J Biochem. 1989 Feb;105(2):312-7. [PubMed ]
5. Yubisui T, Miyata T, Iwanaga S, Tamura M, Takeshita M: Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes. J Biochem (Tokyo). 1986 Feb;99(2):407-22. [PubMed ]
6. Yubisui T, Miyata T, Iwanaga S, Tamura M, Yoshida S, Takeshita M, Nakajima H: Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes. J Biochem (Tokyo). 1984 Aug;96(2):579-82. [PubMed ]
7. Bulbarelli A, Valentini A, DeSilvestris M, Cappellini MD, Borgese N: An erythroid-specific transcript generates the soluble form of NADH-cytochrome b5 reductase in humans. Blood. 1998 Jul 1;92(1):310-9. [PubMed ]
8. Shirabe K, Yubisui T, Nishino T, Takeshita M: Role of cysteine residues in human NADH-cytochrome b5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential. J Biol Chem. 1991 Apr 25;266(12):7531-6. [PubMed ]
9. Yubisui T, Shirabe K, Takeshita M, Kobayashi Y, Fukumaki Y, Sakaki Y, Takano T: Structural role of serine 127 in the NADH-binding site of human NADH-cytochrome b5 reductase. J Biol Chem. 1991 Jan 5;266(1):66-70. [PubMed ]
10. Katsube T, Sakamoto N, Kobayashi Y, Seki R, Hirano M, Tanishima K, Tomoda A, Takazakura E, Yubisui T, Takeshita M, et al.: Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: putative mechanisms of tissue-dependent enzyme deficiency. Am J Hum Genet. 1991 Apr;48(4):799-808. [PubMed ]
11. Shirabe K, Yubisui T, Borgese N, Tang CY, Hultquist DE, Takeshita M: Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J Biol Chem. 1992 Oct 5;267(28):20416-21. [PubMed ]
12. Shirabe K, Fujimoto Y, Yubisui T, Takeshita M: An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme. J Biol Chem. 1994 Feb 25;269(8):5952-7. [PubMed ]
13. Vieira LM, Kaplan JC, Kahn A, Leroux A: Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II. Blood. 1995 Apr 15;85(8):2254-62. [PubMed ]
14. Jenkins MM, Prchal JT: A high-frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans. Hum Genet. 1997 Feb;99(2):248-50. [PubMed ]
15. Wu YS, Huang CH, Wan Y, Huang QJ, Zhu ZY: Identification of a novel point mutation (Leu72Pro) in the NADH-cytochrome b5 reductase gene of a patient with hereditary methaemoglobinaemia type I. Br J Haematol. 1998 Jul;102(2):575-7. [PubMed ]
16. Higasa K, Manabe JI, Yubisui T, Sumimoto H, Pung-Amritt P, Tanphaichitr VS, Fukumaki Y: Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene. Br J Haematol. 1998 Dec;103(4):922-30. [PubMed ]
17. Wang Y, Wu YS, Zheng PZ, Yang WX, Fang GA, Tang YC, Xie F, Lan FH, Zhu ZY: A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia. Blood. 2000 May 15;95(10):3250-5. [PubMed ]

MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTPYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYPLLRNHPEPTLDQLTDALGGNLCRCHGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMADKQSQRTRVFGSER
MMWFSPVTLKDLLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPGYNSPDRIEEPECCKPC
IYGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPISR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAVLITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLAS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI

• Nicotinate and Nicotinamide Metabolism (map00760 )
• Tryptophan Metabolism (map00380 )
• Tyrosine Metabolism (map00350 )
• Valine, Leucine and Isoleucine Degradation (map00280 )
• Vitamin B6 Metabolism (map00750 )

• an aldehyde + H2O + O2 = a carboxylic acid + H2O2

• Ald_Xan_dh_C (PF01315 )
• Ald_Xan_dh_C2 (PF02738 )
• CO_deh_flav_C (PF03450 )
• FAD_binding_5 (PF00941 )
• Fer2 (PF00111 )
• Fer2_2 (PF01799 )

• None

• None

ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
CCGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACCCCCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCCATGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGATAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGACCTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGGTTATAATTCTCCTGATAGAATTGAAGAACCTGAGTGTTGTAAACCATGC
ATATATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCATCTCAAGG
AAGTGGGAATTTGTGTCAGCCTTCCGACAAGCCCAGCGACAGGAGAATGCGCTAGCGATA
GTCAATTCAGGAATGAGAGTCTTTTTTGGAGAAGGGGATGGCATTATTAGAGAGTTATGC
ATCTCATATGGAGGCGTTGGTCCAGCCACCATCTGTGCCAAGAATTCCTGCCAGAAACTC
ATTGGAAGGCACTGGAACGAACAGATGCTGGATATAGCCTGCAGGCTTATTCTGAATGAA
GTCTCCCTTTTGGGCTCGGCGCCAGGTGGGAAAGTGGAGTTCAAGAGGACTCTCATCATC
AGCTTCCTCTTCAAGTTCTACCTGGAAGTGTCACAGATTTTGAAAAAGATGGATCCAGTT
CACTATCCTAGCCTTGCAGACAAGTATGAAAGTGCTTTAGAAGATCTTCATTCCAAACAT
CACTGCAGTACATTAAAGTACCAGAATATAGGCCCAAAGCAGCATCCTGAAGACCCAATT
GGCCACCCCATCATGCATCTGTCTGGTGTGAAGCATGCCACGGGGGAGGCCATCTACTGT
GATGACATGCCTCTGGTGGACCAGGAACTTTTCTTGACTTTTGTGACTAGTTCAAGAGCT
CATGCTAAGATTGTGTCTATTGATCTGTCAGAAGCTCTCAGCATGCCCGGTGTGGTGGAC
ATCATGACAGCAGAACATCTTAGTGACGTCAACTCCTTCTGCTTTTTTACTGAAGCTGAG
AAATTTCTGGCGACAGATAAGGTGTTCTGTGTGGGTCAGCTTGTCTGTGCTGTGCTTGCC
GATTCTGAGGTTCAGGCAAAGCGAGCTGCTAAGCGAGTGAAGATTGTCTATCAAGACTTG
GAGCCGCTGATACTAACAATTGAGGAAAGTATACAACACAACTCCTCCTTCAAGCCAGAA
AGGAAACTGGAATATGGAAATGTTGACGAAGCATTTAAAGTGGTTGATCAAATTCTTGAA
GGTGAAATACATATGGGAGGTCAAGAACATTTTTATATGGAAACCCAAAGCATGCTTGTC
GTTCCCAAGGGAGAGGATCAAGAAATGGATGTCTACGTGTCCACACAGTTTCCCAAATAT
ATACAGGACATTGTTGCCTCAACCTTGAAGCTCCCAGCTAACAAGGTCATGTGCCATGTA
AGGCGTGTTGGTGGAGCGTTTGGAGGGAAGGTGTTAAAAACCGGAATCATTGCAGCCGTC
ACTGCATTTGCCGCAAACAAACATGGCCGTGCAGTTCGCTGTGTTCTGGAACGAGGAGAA
GACATGTTAATAACTGGAGGCCGCCATCCTTACCTTGGAAAGTACAAAGCTGGATTCATG
AACGATGGCAGAATCTTGGCCCTGGACATGGAGCATTACAGCAATGCAGGCGCCTCCTTG
GATGAATCATTATTCGTGATAGAAATGGGACTTCTGAAAATGGACAATGCTTACAAGTTT
CCCAATCTCCGCTGCCGGGGTTGGGCATGCAGAACCAACCTTCCATCCAACACAGCTTTT
CGTGGGTTTGGCTTTCCTCAGGCAGTGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGCGTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA

1. Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10690-4. [PubMed ]

1. NADH-ubiquinone oxidoreductase MWFE subunit
2. Complex I-MWFE
3. CI-MWFE

MWFEILPGLSVMGVCLLIPGLATAYIHRFTNGGKEKRVAHFGYHWSLMERDRRISGVDRY
YVSKGLENID

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• 1-24

ATGTGGTTCGAGATTCTCCCCGGACTCTCCGTCATGGGCGTGTGCTTGTTGATTCCAGGA
CTGGCTACTGCGTACATCCACAGGTTCACTAACGGGGGCAAGGAAAAAAGGGTTGCTCAT
TTTGGGTATCACTGGAGTCTGATGGAAAGAGATAGGCGCATCTCTGGAGTTGATCGTTAC
TATGTGTCAAAGGGTTTGGAGAACATTGATTAA

1. Zhuchenko O, Wehnert M, Bailey J, Sun ZS, Lee CC: Isolation, mapping, and genomic structure of an X-linked gene for a subunit of human mitochondrial complex I. Genomics. 1996 Nov 1;37(3):281-8. [PubMed ]
2. Frattini A, Faranda S, Bagnasco L, Patrosso C, Nulli P, Zucchi I, Vezzoni P: Identification of a new member (ZNF183) of the Ring finger gene family in Xq24-25. Gene. 1997 Jun 19;192(2):291-8. [PubMed ]

1. NADH-ubiquinone oxidoreductase MLRQ subunit homolog
2. NUOMS

MAGASLGARFYRQIKRHPGIIPMIGLICLGMGSAALYLLRLALRSPDVCWDRKNNPEPWN
RLSPNDQYKFLAVSTDYKKLKKDRPDF

• 1-35

ATGGCAGGAGCCAGTCTTGGGGCCCGCTTCTACCGGCAGATCAAAAGACATCCGGGGATC
ATCCCGATGATCGGCTTAATCTGCCTGGGCATGGGCAGCGCTGCGCTTTACTTGCTGCGA
CTCGCCCTTCGCAGCCCCGACGTCTGCTGGGACAGAAAGAACAACCCGGAGCCCTGGAAC
CGCCTGAGCCCCAATGACCAATACAAGTTCCTTGCAGTTTCCACTGACTATAAGAAGCTG
AAGAAGGACCGGCCAGACTTCTAA

1. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

1. NADH-ubiquinone oxidoreductase B9 subunit
2. Complex I-B9
3. CI-B9

MAARVGAFLKNAWDKEPVLVVSFVVGGLAVILPPLSPYFKYSVMINKATPYNYPVPVRDD
GNMPDVPSHPQDPQGPSLEWLKKL

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• 1-29

ATGGCTGCGAGAGTCGGCGCCTTCCTCAAGAATGCCTGGGACAAGGAGCCAGTGCTGGTC
GTGTCCTTCGTCGTCGGGGGCCTCGCTGTAATTCTGCCCCCATTGAGCCCCTACTTCAAG
TACTCCGTCATGATCAACAAGGCCACGCCCTACAACTACCCAGTGCCCGTCCGTGATGAT
GGGAACATGCCCGACGTGCCCAGCCACCCCCAGGACCCTCAGGGCCCCAGCCTGGAGTGG
CTGAAGAAACTGTGA

1. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]
2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]

1. NADH dehydrogenase subunit 4L

MPLIYMNIMLAFTISLLGMLVYRSHLMSSLLCLEGMMLSLFIMATLMTLNTHSLLANIVP
IAMLVFAACEAAVGLALLVSISNTYGLDYVHNLNLLQC

• Oxidative phosphorylation (map00190 )
• Ubiquinone Biosynthesis (map00130 )

• NADH + H+ + ubiquinone = NAD+ + ubiquinol

• Oxidored_q2 (PF00420 )

• 1-18

• 26-48
• 58-80

1. Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
2. Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
3. Arnason U, Xu X, Gullberg A: Comparison between the complete mitochondrial DNA sequences of Homo and the common chimpanzee based on nonchimeric sequences. J Mol Evol. 1996 Feb;42(2):145-52. [PubMed ]
4. Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
5. Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
6. Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
7. Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
8. Brown MD, Torroni A, Reckord CL, Wallace DC: Phylogenetic analysis of Leber's hereditary optic neuropathy mitochondrial DNA's indicates multiple independent occurrences of the common mutations. Hum Mutat. 1995;6(4):311-25. [PubMed ]
9. Polyak K, Li Y, Zhu H, Lengauer C, Willson JK, Markowitz SD, Trush MA, Kinzler KW, Vogelstein B: Somatic mutations of the mitochondrial genome in human colorectal tumours. Nat Genet. 1998 Nov;20(3):291-3. [PubMed ]

1. NADH-ubiquinone oxidoreductase subunit B14.7
2. Complex I-B14.7
3. CI-B14.7

MAPKVFRQYWDIPDGTDCHRKAYSTTSIASVAGLTAAAYRVTLNPPGTFLEGVAKVGQYT
FTAAAVGAVFGLTTCISAHVREKPDDPLNYFLGGCAGGLTLGARTHNYGIGAAACVYFGI
AASLVKMGRLEGWEVFAKPKV

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• None

• 21-43 58-80

ATGGCGCCGAAGGTTTTTCGTCAGTACTGGGATATCCCCGATGGCACCGATTGCCACCGC
AAAGCCTACAGCACCACCAGTATTGCCAGCGTCGCTGGCCTGACCGCCGCTGCCTACAGA
GTCACACTCAATCCTCCGGGCACCTTCCTTGAAGGAGTGGCTAAGGTTGGACAATACACG
TTCACTGCAGCTGCTGTCGGGGCCGTGTTTGGCCTCACCACCTGCATCAGCGCCCATGTC
CGCGAGAAGCCCGACGACCCCCTGAACTACTTCCTCGGTGGCTGCGCCGGAGGCCTGACT
CTGGGAGCACGCACGCACAACTACGGGATTGGCGCCGCCGCCTGCGTGTACTTTGGCATA
GCGGCCTCCCTGGTCAAGATGGGCCGGCTGGAGGGCTGGGAGGTGTTTGCAAAACCCAAG
GTGTGA

1. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]

1. TR
2. TR1

MNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCV
NVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVAL
REKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISS
DDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHM
EEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKI
GLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAG
STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNK
CYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFT
TLSVTKRSGASILQAGCCG

• Pyrimidine Metabolism (map00240 )

• thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+

• Pyr_redox (PF00070 )
• Pyr_redox_2 (PF07992 )
• Pyr_redox_dim (PF02852 )

• None

• None

ATGAACGGCCCTGAAGATCTTCCCAAGTCCTATGACTATGACCTTATCATCATTGGAGGT
GGCTCAGGAGGTCTGGCAGCTGCTAAGGAGGCAGCCCAATATGGCAAGAAGGTGATGGTC
CTGGACTTTGTCACTCCCACCCCTCTTGGAACTAGATGGGGTCTTGGAGGAACATGTGTG
AATGTGGGTTGCATACCTAAAAAACTGATGCATCAAGCAGCTTTGTTAGGACAAGCCCTG
CAAGACTCTCGAAATTATGGATGGAAAGTCGAGGAGACAGTTAAGCATGATTGGGACAGA
ATGATAGAAGCTGTACAGAATCACATTGGCTCTTTGAATTGGGGCTACCGAGTAGCTCTG
CGGGAGAAAAAAGTCGTCTATGAGAATGCTTATGGGCAATTTATTGGTCCTCACAGGATT
AAGGCAACAAATAATAAAGGCAAAGAAAAAATTTATTCAGCAGAGAGTTTTCTCATTGCC
ACTGGTGAAAGACCACGTTACTTGGGCATCCCTGGTGACAAAGAATACTGCATCAGCAGT
GATGATCTTTTCTCCTTGCCTTACTGCCCGGGTAAGACCCTGGTTGTTGGAGCATCCTAT
GTCGCTTTGGAGTGCGCTGGATTTCTTGCTGGTATTGGTTTAGGCGTCACTGTTATGGTT
AGGTCCATTCTTCTTAGAGGATTTGACCAGGACATGGCCAACAAAATTGGTGAACACATG
GAAGAACATGGCATCAAGTTTATAAGACAGTTCGTACCAATTAAAGTTGAACAAATTGAA
GCAGGGACACCAGGCCGACTCAGAGTAGTAGCTCAGTCCACCAATAGTGAGGAAATCATT
GAAGGAGAATATAATACGGTGATGCTGGCAATAGGAAGAGATGCTTGCACAAGAAAAATT
GGCTTAGAAACCGTAGGGGTGAAGATAAATGAAAAGACTGGAAAAATACCTGTCACAGAT
GAAGAACAGACCAATGTGCCTTACATCTATGCCATTGGCGATATATTGGAGGATAAGGTG
GAGCTCACCCCAGTTGCAATCCAGGCAGGAAGATTGCTGGCTCAGAGGCTCTATGCAGGT
TCCACTGTCAAGTGTGACTATGAAAATGTTCCAACCACTGTATTTACTCCTTTGGAATAT
GGTGCTTGTGGCCTTTCTGAGGAGAAAGCTGTGGAGAAGTTTGGGGAAGAAAATATTGAG
GTTTACCATAGTTACTTTTGGCCATTGGAATGGACGATTCCGTCAAGAGATAACAACAAA
TGTTATGCAAAAATAATCTGTAATACTAAAGACAATGAACGTGTTGTGGGCTTTCACGTA
CTGGGTCCAAATGCTGGAGAAGTTACACAAGGCTTTGCAGCTGCGCTCAAATGTGGACTG
ACCAAAAAGCAGCTGGACAGCACAATTGGAATCCACCCTGTCTGTGCAGAGGTATTCACA
ACATTGTCTGTGACCAAGCGCTCTGGGGCAAGCATCCTCCAGGCTGGCTGCTGA

1. Gasdaska PY, Gasdaska JR, Cochran S, Powis G: Cloning and sequencing of a human thioredoxin reductase. FEBS Lett. 1995 Oct 2;373(1):5-9. [PubMed ]

1. Lathosterol 5-desaturase
2. Delta(7-sterol 5-desaturase
3. C-5 sterol desaturase
4. Sterol-C5- desaturase

MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE

• Sterol_desat (PF01598 )

• None

• 32-52 79-99 117-137 186-206

ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTAAGAATGAAAAATTAT
TCAATGGAGAGTTTACAAAGACTGAATAGATTATTGCCCAGTTATTCTTAA

1. Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed ]
2. Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed ]
3. Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed ]
4. Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed ]
5. Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed ]

1. NADH-ubiquinone oxidoreductase 18 kDa subunit
2. Complex I-18 kDa
3. CI-18 kDa
4. Complex I-AQDQ
5. CI- AQDQ

MAAVSMSVVLRQTLWRRRAVAVAALSVSRVPTRSLRTSTWRLAQDQTQDTQLITVDEKLD
ITTLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADP
LSNMVLTFSTKEDAVSFAEKNGWSYDIEERKVPKPKSKSYGANFSWNKRTRVSTK

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• ETC_C1_NDUFA4 (PF04800 )

• 1-34

ATGGCGGCGGTCTCAATGTCAGTGGTACTGAGGCAGACGTTGTGGCGGAGAAGGGCAGTG
GCTGTAGCTGCCCTTTCCGTTTCCAGGGTTCCGACCAGGTCGTTGAGGACTTCCACATGG
AGATTGGCACAGGACCAGACTCAAGACACACAACTCATAACAGTTGATGAAAAATTGGAT
ATCACTACTTTAACTGGCGTTCCAGAAGAGCATATAAAAACTAGAAAAGTCAGGATCTTT
GTTCCTGCTCGCAATAACATGCAGTCTGGAGTAAACAACACAAAGAAATGGAAGATGGAG
TTTGATACCAGGGAGCGATGGGAAAATCCTTTGATGGGTTGGGCATCAACGGCTGATCCC
TTATCCAACATGGTTCTAACCTTCAGTACTAAAGAAGATGCAGTTTCCTTTGCAGAAAAA
AATGGATGGAGCTATGACATTGAAGAGAGGAAGGTTCCAAAACCCAAGTCCAAGTCTTAT
GGTGCAAACTTTTCTTGGAACAAAAGAACAAGAGTATCCACAAAATAG

1. van den Heuvel L, Ruitenbeek W, Smeets R, Gelman-Kohan Z, Elpeleg O, Loeffen J, Trijbels F, Mariman E, de Bruijn D, Smeitink J: Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit. Am J Hum Genet. 1998 Feb;62(2):262-8. [PubMed ]

1. NRH dehydrogenase [quinone] 2
2. Quinone reductase 2
3. QR2
4. NRH:quinone oxidoreductase 2

MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNFEPRATDKDITGTL
SNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRV
LCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFC
GFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ

• Flavodoxin_2 (PF02525 )

• None

• None

ATGGCAGGTAAGAAAGTACTCATTGTCTATGCACACCAGGAACCCAAGTCTTTCAACGGA
TCCTTGAAGAATGTGGCTGTAGATGAACTGAGCAGGCAGGGCTGCACCGTCACAGTGTCT
GATTTGTATGCCATGAACTTTGAGCCGAGGGCCACAGACAAAGATATCACTGGTACTCTT
TCTAATCCTGAGGTTTTCAATTATGGAGTGGAAACCCACGAAGCCTACAAGCAAAGGTCT
CTGGCTAGCGACATCACTGATGAGCAGAAAAAGGTTCGGGAGGCTGACCTAGTGATATTT
CAGTTCCCGCTGTACTGGTTCAGCGTGCCGGCCATCCTGAAGGGCTGGATGGATAGGGTG
CTGTGCCAGGGCTTTGCCTTTGACATCCCAGGATTCTACGATTCCGGTTTGCTCCAGGGT
AAACTAGCGCTCCTTTCCGTAACCACGGGAGGCACGGCCGAGATGTACACGAAGACAGGA
GTCAATGGAGATTCTCGATACTTCCTGTGGCCACTCCAGCATGGCACATTACACTTCTGT
GGATTTAAAGTCCTTGCCCCTCAGATCAGCTTTGCTCCTGAAATTGCATCCGAAGAAGAA
AGAAAGGGGATGGTGGCTGCGTGGTCCCAGAGGCTGCAGACCATCTGGAAGGAAGAGCCC
ATCCCCTGCACAGCCCACTGGCACTTCGGGCAATAA

1. Jaiswal AK, Burnett P, Adesnik M, McBride OW: Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6. Biochemistry. 1990 Feb 20;29(7):1899-906. [PubMed ]
2. Jaiswal AK: Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression. J Biol Chem. 1994 May 20;269(20):14502-8. [PubMed ]
3. Wu K, Knox R, Sun XZ, Joseph P, Jaiswal AK, Zhang D, Deng PS, Chen S: Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch Biochem Biophys. 1997 Nov 15;347(2):221-8. [PubMed ]
4. Zhao Q, Yang XL, Holtzclaw WD, Talalay P: Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase) Proc Natl Acad Sci U S A. 1997 Mar 4;94(5):1669-74. [PubMed ]
5. Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM: Crystal structure of human quinone reductase type 2, a metalloflavoprotein. Biochemistry. 1999 Aug 3;38(31):9881-6. [PubMed ]

1. NADH-ubiquinone oxidoreductase 15 kDa subunit
2. Complex I-15 kDa
3. CI-15 kDa

MPFLDIQKRFGLNIDRWLTIQSGEQPYKMAGRCHAFEKEWIECAHGIGYTRAEKECKIEY
DDFVECLLRQKTMRRAGTIRKQRDKLIKEGKYTPPPHHIGKGEPRP

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• None

• None

ATGCCTTTCTTGGACATCCAGAAAAGGTTCGGCCTTAACATAGATCGATGGTTGACAATC
CAGAGTGGTGAACAGCCCTACAAGATGGCTGGTCGATGCCATGCTTTTGAAAAAGAATGG
ATAGAATGTGCACATGGAATCGGTTATACTCGGGCAGAGAAAGAGTGCAAGATAGAATAT
GATGATTTCGTAGAGTGTTTGCTTCGGCAGAAAACGATGAGACGTGCAGGTACCATCAGG
AAGCAGCGGGATAAGCTGATAAAGGAAGGAAAGTACACCCCTCCACCTCACCACATTGGC
AAGGGGGAGCCTCGGCCCTGA

1. Mao M, Fu G, Wu JS, Zhang QH, Zhou J, Kan LX, Huang QH, He KL, Gu BW, Han ZG, Shen Y, Gu J, Yu YP, Xu SH, Wang YX, Chen SJ, Chen Z: Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8175-80. [PubMed ]
2. Loeffen J, Smeets R, Smeitink J, Triepels R, Sengers R, Trijbels F, van den Heuvel L: The human NADH: ubiquinone oxidoreductase NDUFS5 (15 kDa) subunit: cDNA cloning, chromosomal localization, tissue distribution and the absence of mutations in isolated complex I-deficient patients. J Inherit Metab Dis. 1999 Feb;22(1):19-28. [PubMed ]

1. NADH-ubiquinone oxidoreductase 24 kDa subunit

MFFSAALRARAAGLTAHWGRHVRNLHKTVMQNGAGGALFVHRDTPENNPDTPFDFTPENY
KRIEAIVKNYPEGHKAAAVLPVLDLAQRQNGWLPISAMNKVAEVLQVPPMRVYEVATFYT
MYNRKPVGKYHIQVCTTTPCMLRNSDSILEAIQKKLGIKVGETTPDKLFTLIEVECLGAC
VNAPMVQINDNYYEDLTAKDIEEIIDELKAGKIPKPGPRSGRFSCEPAGGLTSLTEPPKG
PGFGVQAGL

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• Complex1_24kDa (PF01257 )

• 1-11

ATGTTCTTCTCCGCGGCGCTCCGGGCCCGGGCGGCTGGCCTCACCGCCCACTGGGGAAGA
CATGTAAGGAATTTGCATAAGACAGCTATGCAAAATGGAGCTGGAGGAGCTTTATTTGTG
CACAGAGATACTCCTGAGAATAACCCTGATACTCCATTTGATTTCACACCAGAAAACTAT
AAGAGGATAGAGGCAATTGTAAAAAACTATCCAGAAGGCCATAAAGCAGCAGCTGTTCTT
CCAGTCCTGGATTTAGCCCAAAGGCAGAATGGGTGGTTGCCCATCTCTGCTATGAACAAG
GTTGCAGAAGTTTTACAAGTACCTCCAATGAGAGTATATGAAGTAGCAACTTTTTATACA
ATGTATAATCGAAAGCCAGTTGGAAAGTATCACATTCAGGTCTGCACTACTACACCCTGC
ATGCTTCGAAACTCTGACAGCATACTGGAGGCCATTCAGAAAAAGCTTGGAATAAAGGTT
GGGGAGACTACACCTGACAAACTTTTCACTCTTATAGAAGTGGAATGTTTAGGGGCCTGT
GTGAACGCACCAATGGTTCAAATAAATGACAATTACTATGAGGATTTGACAGCTAAGGAT
ATTGAAGAAATTATTGATGAGCTCAAGGCTGGCAAAATCCCAAAACCAGGGCCAAGGAGT
GGACGCTTCTCTTGTGAGCCAGCTGGAGGTCTTACCTCTTTGACTGAACCACCCAAGGGA
CCTGGATTTGGTGTACAAGCAGGCCTTTAA

1. Pilkington SJ, Walker JE: Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of import precursors of the bovine and human 24-kDa subunit. Biochemistry. 1989 Apr 18;28(8):3257-64. [PubMed ]

1. Hepatic flavin-containing monooxygenase 5
2. FMO 5
3. Dimethylaniline oxidase 5

MTKKRIAVIGGGVSGLSSIKCCVEEGLEPVCFERTDDIGGLWRFQENPEEGRASIYKSVI
INTSKEMMCFSDYPIPDHYPNFMHNAQVLEYFRMYAKEFDLLKYIRFKTTVCSVKKQPDF
ATSGQWEVVTESEGKKEMNVFDGVMVCTGHHTNAHLPLESFPGIEKFKGQYFHSRDYKNP
EGFTGKRVIIIGIGNSGGDLAVEISQTAKQVFLSTRRGAWILNRVGDYGYPADVLFSSRL
THFIWKICGQSLANKYLEKKINQRFDHEMFGLKPKHRALSQHPTLNDDLPNRIISGLVKV
KGNVKEFTETAAIFEDGSREDDIDAVIFATGYSFDFPFLEDSVKVVKNKISLYKKVFPPN
LERPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKTLPSQSEMMAEISKAQEEIDKRY
VESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLLLGPCTPIHYRVQGPGK
WDGARKAILTTDDRIRKPLMTRVVERSSSMTSTMTIGKFMLALAFFAIIIAYF

• N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O

• FMO-like (PF00743 )

• None

• 510-532

ATGACTAAGAAAAGAATTGCTGTGATTGGGGGAGGAGTGAGCGGGCTCTCTTCCATCAAG
TGCTGCGTAGAAGAAGGCTTGGAACCTGTCTGCTTTGAAAGGACTGATGACATCGGAGGG
CTCTGGAGGTTCCAGGAAAATCCTGAAGAAGGAAGGGCCAGTATTTACAAATCAGTGATC
ATCAATACTTCTAAAGAGATGATGTGCTTCAGTGACTATCCAATCCCAGATCATTATCCC
AACTTCATGCATAATGCCCAGGTCCTGGAGTATTTCAGGATGTATGCCAAAGAATTTGAC
CTTCTAAAGTATATTCGATTTAAGACCACTGTGTGCAGTGTGAAGAAGCAGCCTGATTTT
GCCACTTCAGGCCAATGGGAAGTGGTCACTGAATCTGAAGGGAAAAAGGAGATGAATGTC
TTTGATGGAGTCATGGTTTGCACTGGCCATCACACCAATGCTCATCTACCTCTGGAAAGC
TTCCCTGGAATTGAGAAGTTCAAAGGGCAGTACTTCCACAGTCGAGACTATAAGAACCCA
GAGGGATTCACTGGAAAGAGAGTCATTATAATTGGCATTGGGAATTCTGGAGGGGATCTG
GCTGTAGAGATTAGCCAAACAGCCAAGCAGGTTTTCCTCAGCACCAGGAGAGGGGCTTGG
ATCCTGAATCGTGTAGGGGACTACGGATATCCTGCTGATGTGTTGTTCTCTTCTCGACTT
ACACATTTTATATGGAAGATCTGTGGCCAATCATTAGCAAACAAATATTTGGAAAAAAAG
ATAAACCAAAGGTTTGACCATGAAATGTTTGGCCTGAAGCCTAAACACAGAGCTCTGAGT
CAGCATCCAACCTTAAATGATGACCTGCCAAATCGTATCATTTCTGGCTTGGTGAAAGTG
AAAGGAAATGTGAAGGAATTCACGGAGACAGCTGCCATATTTGAGGATGGCTCCAGGGAG
GATGACATTGATGCTGTTATCTTTGCCACAGGCTATAGCTTTGACTTTCCATTTCTGGAA
GATTCCGTCAAAGTGGTCAAAAACAAGATATCCCTGTATAAAAAGGTCTTCCCTCCTAAC
CTGGAAAGGCCAACTCTTGCAATCATAGGCTTGATTCAGCCCTTAGGAGCCATTATGCCC
ATTTCAGAGCTCCAAGGACGCTGGGCCACTCAGGTATTTAAAGGTCTAAAGACATTGCCC
TCACAGAGTGAAATGATGGCAGAAATATCTAAAGCTCAAGAGGAAATTGACAAAAGGTAT
GTGGAGAGCCAACGCCATACCATTCAGGGAGACTACATAGATACCATGGAAGAGCTTGCT
GATTTGGTGGGGGTCAGGCCCAATCTGCTGTCTCTGGCCTTCACTGACCCCAAGCTGGCA
TTACACTTATTACTGGGACCCTGCACTCCAATCCACTATCGTGTACAGGGCCCTGGAAAG
TGGGATGGGGCTCGAAAAGCTATCCTCACCACAGATGATCGCATCAGGAAGCCTCTGATG
ACAAGAGTAGTTGAAAGGAGTAGTTCTATGACTTCAACAATGACAATAGGCAAGTTTATG
CTAGCTCTTGCCTTCTTTGCTATAATTATAGCTTACTTCTAG

1. Overby LH, Buckpitt AR, Lawton MP, Atta-Asafo-Adjei E, Schulze J, Philpot RM: Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Arch Biochem Biophys. 1995 Feb 20;317(1):275-84. [PubMed ]
2. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed ]

1. NADH-ubiquinone oxidoreductase 42 kDa subunit
2. Complex I-42kD
3. CI-42kD

MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVI
TVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDD
PRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIR
KQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENA
YKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQD
KFEVLNYTSIPIFLPEVTIGAHQTDRVLHQFRELPGRKYSPGYNTEVGDKWIWLK

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• dNK (PF01712 )

• 1-20

ATGGCCTTGCGGCTCCTGAAGCTGGCAGCGACGTCCGCGTCCGCCCGGGTCGTGGCGGCG
GGCGCCCAGCGCGTGAGAGGAATTCATAGCAGTGTGCAGTGCAAGCTGCGCTATGGAATG
TGGCATTTCCTACTTGGGGATAAAGCAAGCAAAAGACTGACAGAACGCAGCAGAGTGATA
ACTGTAGATGGCAATATATGTACTGGAAAAGGCAAACTTGCAAAAGAAATAGCAGAGAAA
CTAGGCTTCAAGCACTTTCCTGAAGCGGGGATTCATTATCCAGACAGTACCACAGGAGAT
GGGAAGCCCCTCGCCACCGACTATAATGGCAACTGTAGTTTGGAGAAATTTTACGATGAT
CCGAGAAGCAATGATGGCAACAGTTACCGCCTGCAGTCCTGGTTGTACAGCAGTCGCCTG
CTGCAGTACTCAGATGCCTTGGAGCACTTGCTGACCACAGGACAAGGTGTTGTGTTGGAG
CGCTCCATCTTCAGTGACTTTGTGTTCCTGGAGGCGATGTACAACCAGGGATTCATCCGA
AAGCAGTGTGTGGACCACTACAACGAGGTGAAGAGCGTCACCATCTGCGATTACCTGCCC
CCCCACCTGGTGATTTACATCGATGTGCCCGTTCCAGAGGTCCAGAGGCGGATTCAGAAG
AAAGGAGATCCACATGAAATGAAGATCACCTCTGCCTATCTACAGGACATTGAGAATGCC
TATAAGAAAACCTTTCTCCCTGAGATGAGTGAAAAATGTGAGGTTTTACAGTATTCTGCA
AGGGAAGCTCAAGATTCAAAAAAGGTGGTAGAGGACATTGAATACCTGAAGTTCGATAAA
GGGCCGTGGCTCAAGCAGGACAATCGCACTTTATACCACCTGCGATTACTGGTTCAGGAT
AAGTTTGAGGTGCTGAATTACACAAGCATTCCTATCTTTCTCCCGGAAGTCACCATTGGA
GCTCATCAGACTGACCGTGTCTTACATCAGTTCAGAGAGCTGCCGGGCCGCAAGTACAGC
CCTGGGTACAACACCGAGGTGGGAGACAAGTGGATCTGGCTGAAGTGA

1. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]

1. NADH-ubiquinone oxidoreductase B14 subunit
2. Complex I-B14
3. CI-B14

MAGSGVRQATSTASTFVKPIFSRDMNEAKRRVRELYRAWYREVPNTVHQFQLDITVKMGR
DKVREMFMKNAHVTDPRVVDLLVIKGKIELEETIKVWKQRTHVMRFFHETEAPRPKDFLS
KFYVGHDP

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• Complex1_LYR (PF05347 )

• None

• None

ATGGCGGGGAGCGGCGTCCGCCAAGCTACTTCTACCGCCAGCACCTTCGTGAAGCCCATT
TTCAGTCGGGACATGAACGAGGCCAAGCGGAGGGTGCGCGAGCTCTACCGCGCCTGGTAT
CGGGAGGTGCCGAACACTGTGCACCAATTCCAGCTGGACATCACTGTGAAAATGGGACGG
GATAAAGTCCGAGAAATGTTTATGAAGAATGCCCATGTCACAGACCCCAGGGTGGTTGAT
CTTCTGGTCATTAAGGGAAAGATCGAACTGGAAGAAACAATTAAAGTATGGAAGCAGCGG
ACACATGTTATGCGGTTCTTCCATGAAACAGAAGCGCCAAGGCCAAAGGATTTCCTATCC
AAGTTCTATGTTGGCCACGATCCATGA

1. Ton C, Hwang DM, Dempsey AA, Liew CC: Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. Biochem Biophys Res Commun. 1997 Dec 18;241(2):589-94. [PubMed ]
2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

1. Palmitoyl-CoA oxidase
2. AOX
3. Straight-chain acyl-CoA oxidase
4. SCOX

MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRY
EVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQK
EKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGL
GKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYL
KMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIA
IRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIG
QGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF
EGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSP
ESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFS
EKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIR
SDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL

• Fatty Acid Metabolism (map00071 )

• acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2

• ACOX (PF01756 )
• Acyl-CoA_dh_M (PF02770 )

• None

• None

ATGAACCCGGACCTGCGCAGGGAGCGGGATTCCGCCAGCTTCAACCCGGAGCTGCTTACA
CACATCCTGGACGGCAGCCCCGAGAAAACGCGCCGCCGCCGAGAGATCGAGAACATGATC
CTGAACGACCCAGACTTCCAGCATGAGGACTTGAACTTCCTCACTCGCAGCCAGCGTTAT
GAGGTGGCTGTCAGGAAAAGTGCCATCATGGTGAAGAAGATGAGGGAGTTTGGCATCGCT
GACCCTGATGAAATTATGTGGTTTAAAAAACTACATTTGGTCAATTTTGTGGAACCTGTG
GGCCTCAATTACTCCATGTTTATTCCTACCTTGCTGAATCAGGGCACCACTGCTCAGAAA
GAGAAATGGCTGCTTTCATCCAAAGGACTCCAGATAATTGGCACCTACGCCCAGACGGAA
ATGGGCCACGGAACTCACCTTCGAGGCTTGGAAACCACAGCCACGTATGACCCTGAAACC
CAGGAGTTCATTCTCAACAGTCCTACTGTGACCTCCATTAAATGGTGGCCTGGTGGGCTT
GGAAAGACTTCAAATCATGCAATAGTTCTTGCCCAGCTCATCACTAAGGGAAAATGCTAT
GGATTACATGCCTTTATCGTACCTATTCGTGAAAATCGGACCCATAAGCCTTTGCCAGGA
ATTACCGTTGGTGACATCGGCCCCAAATTTGGTTATGATGAGATAGACAATGGCTACCTC
AAAATGGACAACCATCGTATTCCCAGAGAAAACATGCTGATGAAGTATGCCCAGGTGAAG
CCTGATGGACCATACGTGAAACCGCTGAGTAACAAGCTGACTTACGGGACCATGGTGTTT
GTCAGGTCCTTCCTTGTGGGAGAAGCTGCTCGGGCTCTGTCTAAGGCGTGCACCATTGCC
ATCCGATACAGCGCTGTGAGGCACCAGTCTGAAATCAAGCCAGGTGAACCAGAACCACAG
ATTTTGGATTTTCAAACCCAGCAGTATAAACTCTTTCCACTCCTGGCCACTGCCTATGCC
TTCCAGTTTGTGGGCGCATACATGAAGGAGACCTATCACCGGATTAACGAAGGCATTGGT
CAAGGGGACCTGAGTGAACTGCCTGAGCTTCATGCCCTCACCGCTGGACTGAAGGCTTTC
ACCTCCTGGACTGCAAACACTGGCATTGAAGCATGTCGGATGGCTTGTGGTGGGCATGGC
TATTCTCATTGCAGTGGTCTTCCAAATATTTATGTCAATTTCACCCCAAGCTGTACCTTT
GAGGGAGAAAACACTGTCATGATGCTCCAGACGGCTAGGTTCCTGATGAAAAGTTATGAT
CAGGTGCACTCAGGAAAGTTGGTGTGTGGCATGGTGTCCTATTTGAACGACCTGCCCAGT
CAGCGCATCCAGCCACAGCAGGTAGCAGTCTGGCCAACCATGGTGGATATCAACAGCCCC
GAAAGCCTAACCGAAGCATATAAACTCCGTGCAGCCAGATTAGTAGAAATTGCTGCAAAA
AACCTTCAAAAAGAAGTGATTCACAGAAAAAGCAAGGAGGTAGCTTGGAACCTAACTTCT
GTTGACCTTGTTCGAGCAAGTGAGGCACATTTGCACTATGGGTTAGTTAAGCTCTTTTCA
GAAAAACTCCTCAAAATTCAAGATAAAGCCATTCAAGCTGTCTTAAGGAGTTTATGTCTG
CTGTATTCTCTGTATGGAATCAGTCAGAACGCGGGGGATTTCCTTCAGGGGAGCATCATG
ACAGAGCCTCAGATTACACAAGTAAACCAGCGTGTAAAGGAGTTACTCACTCTGATTCGC
TCAGATGCTGTTGCTTTGGTTGATGCATTTGATTTTCAGGATGTGACACTTGGCTCTGTG
CTTGGCCGCTATGATGGGAATGTGTATGAAAACTTGTTTGAGTGGGCTAAGAACTCCCCA
CTGAACAAAGCAGAGGTCCACGAATCTTACAAGCACCTGAAGTCACTGCAGTCCAAGCTC
TGA

1. Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK: Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3107-11. [PubMed ]
2. Chu R, Varanasi U, Chu S, Lin Y, Usuda N, Rao MS, Reddy JK: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [PubMed ]
3. Fournier B, Saudubray JM, Benichou B, Lyonnet S, Munnich A, Clevers H, Poll-The BT: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest. 1994 Aug;94(2):526-31. [PubMed ]
4. Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T: Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8. [PubMed ]

1. DASOX
2. DDO

MDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTP
IHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMT
EAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVV
NCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKG
DWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPV
VHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL

• D-aspartate + H2O + O2 = oxaloacetate + ammonia + H2O2

• DAO (PF01266 )

• 1-19

ATGGACACAGCACGGATTGCAGTTGTCGGGGCAGGTGTGGTGGGGCTCTCCACGGCTGTG
TGCATCTCCAAACTGGTGCCCCGATGCTCCGTTACCATCATTTCAGACAAGTTTACTCCA
GATACCACCAGTGATGTGGCAGCCGGAATGCTTATTCCTCACACTTATCCAGATACACCC
ATTCACACGCAGAAGCAGTGGTTCAGAGAAACCTTTAATCACCTCTTTGCAATTGCCAAT
TCTGCAGAAGCTGGAGATGCTGGTGTTCATTTGGTATCAGGTTGGCAGATATTTCAGAGC
ACTCCGACTGAAGAAGTGCCATTCTGGGCTGACGTGGTTCTGGGATTTCGAAAGATGACT
GAGGCTGAGCTGAAGAAATTCCCCCAGTATGTGTTTGGTCAGGCTTTTACAACCCTGAAA
TGTGAATGCCCTGCCTACCTCCCGTGGTTGGAGAAAAGGATAAAGGGAAGTGGAGGCTGG
ACACTCACTCGGCGAATAGAAGACCTGTGGGAACTTCATCCGTCCTTTGACATCGTGGTC
AACTGTTCAGGCCTTGGAAGCAGACAGCTTGCAGGAGACTCAAAGATTTTCCCTGTAAGG
GGCCAAGTCCTCCAAGTTCAGGCTCCCTGGGTGGAGCATTTTATCCGAGATGGCAGTGGG
CTGACATATATTTATCCTGGTACATCCCATGTAACCCTAGGTGGAACTAGGCAAAAAGGG
GACTGGAATCTGTCCCCGGATGCAGAAAATAGCAGAGAGATTCTTTCCCGATGCTGTGCT
CTGGAGCCCTCCCTCCACGGAGCCTGCAACATCAGGGAGAAGGTGGGCTTGAGGCCCTAC
AGGCCAGGCGTGCGACTGCAGACAGAGCTCCTTGCGCGAGATGGACAGAGGCTGCCTGTA
GTCCACCACTATGGCCATGGGAGTGGGGGCATCTCAGTGCACTGGGGCACTGCTCTGGAG
GCCGCCAGGCTGGTGAGCGAGTGTGTCCATGCCCTCAGGACCCCCATTCCCAAGTCAAAC
CTGTAG

1. Setoyama C, Miura R: Structural and functional characterization of the human brain D-aspartate oxidase. J Biochem (Tokyo). 1997 Apr;121(4):798-803. [PubMed ]
2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]

1. NADH-ubiquinone oxidoreductase B15 subunit
2. Complex I-B15
3. CI-B15

MSFPKYKPSSLRTLPETLDPAEYNISPETRRAQAERLAIRAQLKREYLLQYNDPNRRGLI
ENPALLRWAYARTINVYPNFRPTPKNSLMGALCGFGPLIFIYYIIKTERDRKEKLIQEGK
LDRTFHLSY

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• NDUF_B4 (PF07225 )

• None

• 88-105

ATGTCGTTCCCAAAGTATAAGCCGTCGAGCCTGCGCACTCTGCCTGAGACCCTCGACCCA
GCCGAATACAACATATCTCCGGAAACCCGGCGGGCGCAAGCCGAGCGGTTGGCCATAAGA
GCCCAGCTGAAACGAGAGTACCTGCTTCAGTACAACGATCCCAACCGCCGAGGGCTCATC
GAAAATCCTGCCTTGCTTCGTTGGGCCTATGCAAGAACAATAAATGTCTATCCTAATTTC
AGACCCACTCCTAAAAACTCACTCATGGGAGCTCTGTGTGGATTTGGGCCCCTCATCTTC
ATTTATTATATTATCAAAACTGAGAGGGATAGGAAAGAAAAACTTATCCAGGAAGGAAAA
TTGGATCGAACATTTCACCTCTCATATTAA

1. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]

1. Fp
2. Flavoprotein subunit of complex II

MSGVRGLSRLLSARRLALAKAWPTVLQTGTRGFHFTVDGNKRASAKVSDSISAQYPVVDH
EFDAVVVGAGGAGLRAAFGLSEAGFNTACVTKLFPTRSHTVAAQGGINAALGNMEEDNWR
WHFYDTVKGSDWLGDQDAIHYMTEQAPAAVVELENYGMPFSRTEDGKIYQRAFGGQSLKF
GKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIE
DGSIHRIRAKNTVVATGGYGRTYFSCTSAHTSTGDGTAMITRAGLPCQDLEFVQFHPTGI
YGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPE
KDHVYLQLHHLPPEQLATRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQ
VLRHVNGQDQIVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIEESCRPGDK
VPPIKPNAGEESVMNLDKLRFADGSIRTSELRLSMQKSMQNHAAVFRVGSVLQEGCGKIS
KLYGDLKHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDYKVR
IDEYDYSKPIQGQQKKPFEEHWRKHTLSYVDVGTGKVTLEYRPVIDKTLNEADCATVPPA
IRSY

• Citrate Cycle (map00020 )
• Oxidative phosphorylation (map00190 )

• succinate + ubiquinone = fumarate + ubiquinol

• FAD_binding_2 (PF00890 )
• Succ_DH_flav_C (PF02910 )

• 1-19

ATGTCGGGGGTCCGGGGCCTGTCGCGGCTGCTGAGCGCTCGGCGCCTGGCGCTGGCCAAG
GCGTGGCCAACAGTGTTGCAAACAGGAACCCGAGGTTTTCACTTCACTGTTGATGGGAAC
AAGAGGGCATCTGCTAAAGTTTCAGATTCCATTTCTGCTCAGTATCCAGTAGTGGATCAT
GAATTTGATGCAGTGGTGGTAGGCGCTGGAGGGGCAGGCTTGCGAGCTGCATTTGGCCTT
TCTGAGGCAGGGTTTAATACAGCATGTGTTACCAAGCTGTTTCCTACCAGGTCACACACT
GTTGCAGCACAGGGAGGAATCAATGCTGCTCTGGGGAACATGGAGGAGGACAACTGGAGG
TGGCATTTCTACGACACCGTGAAGGGCTCCGACTGGCTGGGGGACCAGGATGCCATCCAC
TACATGACGGAGCAGGCCCCCGCCGCCGTGGTCGAGCTAGAAAATTATGGCATGCCGTTT
AGCAGAACTGAAGATGGGAAGATTTATCAGCGTGCATTTGGTGGACAGAGCCTCAAGTTT
GGAAAGGGCGGGCAGGCCCATCGGTGCTGCTGTGTGGCTGATCGGACTGGCCACTCGCTA
TTGCACACCTTATATGGACGGTCTCTGCGATATGATACCAGCTATTTTGTGGAGTATTTT
GCCTTGGATCTCCTGATGGAGAACGGGGAGTGCCGTGGTGTCATCGCACTGTGCATAGAG
GACGGGTCCATCCATCGCATAAGAGCAAAGAACACTGTTGTTGCCACAGGAGGCTACGGG
CGCACCTACTTCAGCTGCACGTCTGCCCACACCAGCACTGGCGACGGCACGGCCATGATC
ACCAGGGCAGGCCTTCCTTGCCAGGACCTAGAGTTTGTTCAGTTCCACCCTACAGGCATA
TATGGTGCTGGTTGTCTCATTACGGAAGGATGTCGTGGAGAGGGAGGCATTCTCATTAAC
AGTCAAGGCGAAAGGTTTATGGAGCGATACGCCCCTGTCGCGAAGGACCTGGCGTCTAGA
GATGTGGTGTCTCGGTCCATGACTCTGGAGATCCGAGAAGGAAGAGGCTGTGGCCCTGAG
AAAGATCACGTCTACCTGCAGCTGCACCACCTACCTCCAGAGCAGCTGGCCACGCGCCTG
CCTGGCATTTCAGAGACAGCCATGATCTTCGCTGGCGTGGACGTCACGAAGGAGCCGATC
CCTGTCCTCCCCACCGTGCATTATAACATGGGCGGCATTCCCACCAACTACAAGGGGCAG
GTCCTGAGGCACGTGAATGGCCAGGATCAGATTGTGCCCGGCCTGTACGCCTGTGGGGAG
GCCGCCTGTGCCTCGGTACATGGTGCCAACCGCCTCGGGGCAAACTCGCTCTTGGACCTG
GTTGTCTTTGGTCGGGCATGTGCCCTGAGCATCGAAGAGTCATGCAGGCCTGGAGATAAA
GTCCCTCCAATTAAACCAAACGCTGGGGAAGAATCTGTCATGAATCTTGACAAATTGAGA
TTTGCTGATGGAAGCATAAGAACATCGGAACTGCGACTCAGCATGCAGAAGTCAATGCAA
AATCATGCTGCCGTGTTCCGTGTGGGAAGCGTGTTGCAAGAAGGTTGTGGGAAAATCAGC
AAGCTCTATGGAGACCTAAAGCACCTGAAGACGTTCGACCGGGGAATGGTCTGGAACACG
GACCTGGTGGAGACCCTGGAGCTGCAGAACCTGATGCTGTGTGCGCTGCAGACCATCTAC
GGAGCAGAGGCACGGAAGGAGTCACGGGGCGCGCATGCCAGGGAAGACTACAAGGTGCGG
ATTGATGAGTACGATTACTCCAAGCCCATCCAGGGGCAACAGAAGAAGCCCTTTGAGGAG
CACTGGAGGAAGCACACCCTGTCCTATGTGGACGTTGGCACTGGGAAGGTCACTCTGGAA
TATAGACCCGTGATCGACAAAACTTTGAACGAGGCTGACTGTGCCACCGTCCCGCCAGCC
ATTCGCTCCTACTGA

1. Hirawake H, Wang H, Kuramochi T, Kojima S, Kita K: Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the flavoprotein (Fp) subunit of liver mitochondria. J Biochem (Tokyo). 1994 Jul;116(1):221-7. [PubMed ]
2. Morris AA, Farnsworth L, Ackrell BA, Turnbull DM, Birch-Machin MA: The cDNA sequence of the flavoprotein subunit of human heart succinate dehydrogenase. Biochim Biophys Acta. 1994 Mar 29;1185(1):125-8. [PubMed ]
3. Bourgeron T, Rustin P, Chretien D, Birch-Machin M, Bourgeois M, Viegas-Pequignot E, Munnich A, Rotig A: Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency. Nat Genet. 1995 Oct;11(2):144-9. [PubMed ]
4. Van Coster R, Seneca S, Smet J, Van Hecke R, Gerlo E, Devreese B, Van Beeumen J, Leroy JG, De Meirleir L, Lissens W: Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II. Am J Med Genet A. 2003 Jul 1;120(1):13-8. [PubMed ]

1. NADH-ubiquinone oxidoreductase 23 kDa subunit
2. Complex I-23kD
3. CI-23kD
4. TYKY subunit

MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLL
WTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAI
CPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEE
LLYNKEKLLNNGDKWEAEIAANIQADYLYR

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• Fer4 (PF00037 )

• 1-19

ATGCGCTGCCTGACCACGCCTATGCTGCTGCGGGCCCTGGCCCAGGCTGCACGTGCAGGA
CCTCCTGGTGGCCGGAGCCTCCACAGCAGTGCAGTGGCAGCCACCTACAAGTATGTGAAC
ATGCAGGATCCCGAGATGGACATGAAGTCAGTGACTGACCGGGCAGCCCGCACCCTGCTG
TGGACTGAGCTCTTCCGAGGCCTGGGCATGACCCTGAGCTACCTGTTCCGGGAACCGGCC
ACCATCAACTACCCGTTCGAGAAGGGCCCGCTGAGCCCTCGCTTCCGTGGGGAGCATGCG
CTGCGCCGGTACCCATCCGGGGAGGAGCGTTGCATTGCCTGCAAGCTCTGCGAGGCCATC
TGCCCCGCCCAGGCCATCACCATCGAGGCTGAGCCAAGAGCTGATGGCAGCCGCCGGACC
ACCCGCTATGACATCGACATGACCAAGTGCATCTACTGCGGCTTCTGCCAGGAGGCCTGT
CCCGTGGATGCCATCGTCGAGGGCCCCAACTTTGAGTTCTCCACGGAGACCCATGAGGAG
CTGCTGTACAACAAGGAGAAGTTGCTCAACAACGGGGACAAGTGGGAGGCCGAGATCGCC
GCCAACATCCAGGCTGACTACTTGTATCGGTGA

1. Procaccio V, Depetris D, Soularue P, Mattei MG, Lunardi J, Issartel JP: cDNA sequence and chromosomal localization of the NDUFS8 human gene coding for the 23 kDa subunit of the mitochondrial complex I. Biochim Biophys Acta. 1997 Mar 20;1351(1-2):37-41. [PubMed ]
2. de Sury R, Martinez P, Procaccio V, Lunardi J, Issartel JP: Genomic structure of the human NDUFS8 gene coding for the iron-sulfur TYKY subunit of the mitochondrial NADH:ubiquinone oxidoreductase. Gene. 1998 Jul 17;215(1):1-10. [PubMed ]
3. Loeffen J, Smeitink J, Triepels R, Smeets R, Schuelke M, Sengers R, Trijbels F, Hamel B, Mullaart R, van den Heuvel L: The first nuclear-encoded complex I mutation in a patient with Leigh syndrome. Am J Hum Genet. 1998 Dec;63(6):1598-608. [PubMed ]

1. Squalene epoxidase
2. SE

MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQRSG
SQFALFSDILSGLPFIGFFWAKSPPESENKEQLGARRRRKGTNISETSLIGTAACTSTSS
QNDPEVIIVGAGVLGSALVAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGL
GDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAE
PNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKV
SVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYRISSSETRVLVDIRGEMPRNLREYM
VEKIYPQIPDHLKEPFLEATDNSHLRSMLASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG
MTVAFKDIKLWRKLLKGIPDLYDDAAIFEANKSFYWARKTSHSFVVNILAQALYELFSAT
DDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLALIGHFFAVAIYAVYFCFKSEPW
ITKPRALLSSSAVLYKACSVIFPLIYSEMKYMVH

• Steroid Biosynthesis (map00100 )
• Squalene Biosynthesis (map00900 )

• squalene + AH2 + O2 = (S)-squalene-2,3-epoxide + A + H2O

• DAO (PF01266 )
• SE (PF08491 )

• None

• 20-40 61-81 123-143 546-566

ATGTGGACTTTTCTGGGCATTGCCACTTTCACCTATTTTTATAAGAAGTTCGGGGACTTC
ATCACTTTGGCCAACAGGGAGGTCCTGTTGTGCGTGCTGGTGTTCCTCTCGCTGGGCCTG
GTGCTCTCCTACCGCTGTCGCCACCGAAACGGGGGTCTCCTCGGGCGCCAGCGGAGCGGC
TCCCAGTTCGCCCTCTTCTCGGATATTCTCTCAGGCCTGCCTTTCATTGGCTTCTTCTGG
GCCAAATCCCCCCCTGAATCAGAAAATAAGGAGCAGCTCGGGGCCAGGAGGCGCAGAAAA
GGAACCAATATTTCAGAAACAAGCTTAATAGGAACAGCTGCCTGTACATCAACATCTTCT
CAGAATGACCCAGAAGTTATCATCGTGGGAGCTGGCGTGCTTGGCTCTGCTTTGGTAGCT
GTGCTTTCCAGAGATGGAAGAAAGGTGACAGTCATTGAGAGAGACTTAAAAGAGCCTGAC
AGAATAGTTGGAGAATTCCTGCAGCCGGGTGGTTATCATGTTCTCAAAGACCTTGGTCTT
GGAGATACAGTGGAAGGTCTTGATGCCCAGGTTGTAAATGGTTACATGATTCATGATCAG
GAAAGCAAATCAGAGGTTCAGATTCCTTACCCTCTGTCAGAAAACAATCAAGTGCAGAGT
GGAAGAGCTTTCCATCACGGAAGATTCATCATGAGTCTCCGGAAAGCAGCTATGGCAGAG
CCCAATGCAAAGTTTATTGAAGGTGTTGTGTTACAGTTATTAGAGGAAGATGATGTTGTG
ATGGGAGTTCAGTACAAGGATAAAGAGACTGGAGATATCAAGGAACTCCATGCTCCACTG
ACTGTTGTTGCAGATGGGCTTTTCTCCAAGTTCAGGAAAAGCCTGGTCTCCAATAAAGTT
TCTGTATCATCTCATTTTGTTGGCTTTCTTATGAAGAATGCACCACAGTTTAAAGCAAAT
CATGCTGAACTTATTTTAGCTAACCCGAGTCCAGTTCTCATCTACCGGATTTCATCCAGT
GAAACTCGAGTACTTGTTGACATTAGAGGAGAAATGCCAAGGAATTTAAGAGAATACATG
GTTGAAAAAATTTACCCACAAATACCTGATCACCTGAAAGAACCATTCTTAGAAGCCACT
GACAATTCTCATCTGAGGTCCATGCTAGCAAGCTTCCTTCCTCCTTCATCAGTGAAGAAA
CGAGGTGTTCTTCTTTTGGGAGACGCATATAATATGAGGCATCCACTTACTGGTGGAGGA
ATGACTGTTGCTTTTAAAGATATAAAACTATGGAGAAAACTGCTAAAGGGTATCCCTGAC
CTTTATGATGATGCAGCTATTTTCGAGGCCAACAAATCATTTTACTGGGCAAGAAAAACA
TCTCATTCCTTTGTCGTGAATATCCTTGCTCAGGCTCTTTATGAATTATTTTCTGCCACA
GATGATTCCCTGCATCAACTAAGAAAAGCCTGTTTTCTTTATTTCAAACTTGGTGGCGAA
TGTGTTGCGGGTCCTGTTGGGCTGCTTTCTGTATTGTCTCCTAACCCTCTAGCTTTAATT
GGACACTTCTTTGCTGTTGCAATCTATGCCGTGTATTTTTGCTTTAAGTCAGAACCTTGG
ATTACAAAACCTCGAGCCCTTCTCAGTAGTAGTGCTGTATTGTACAAAGCGTGTTCTGTA
ATATTTCCTCTAATTTACTCAGAAATGAAGTATATGGTTCATTAA

1. Nagai M, Sakakibara J, Wakui K, Fukushima Y, Igarashi S, Tsuji S, Arakawa M, Ono T: Localization of the squalene epoxidase gene (SQLE) to human chromosome region 8q24.1. Genomics. 1997 Aug 15;44(1):141-3. [PubMed ]
2. Nakamura Y, Sakakibara J, Izumi T, Shibata A, Ono T: Transcriptional regulation of squalene epoxidase by sterols and inhibitors in HeLa cells. J Biol Chem. 1996 Apr 5;271(14):8053-6. [PubMed ]

1. NADH dehydrogenase subunit 2

MNPLAQPVIYSTIFAGTLITALSSHWFFTWVGLEMNMLAFIPVLTKKMNPRSTEAAIKYF
LTQATASMILLMAILFNNMLSGQWTMTNTTNQYSSLMIMMAMAMKLGMAPFHFWVPEVTQ
GTPLTSGLLLLTWQKLAPISIMYQISPSLNVSLLLTLSILSIMAGSWGGLNQTQLRKILA
YSSITHMGWMMAVLPYNPNMTILNLTIYIILTTTAFLLLNLNSSTTTLLLSRTWNKLTWL
TPLIPSTLLSLGGLPPLTGFLPKWAIIEEFTKNNSLIIPTIMATITLLNLYFYLRLIYST
SITLLPMSNNVKMKWQFEHTKPTPFLPTLIALTTLLLPISPFMLMIL

• Oxidative phosphorylation (map00190 )
• Ubiquinone Biosynthesis (map00130 )

• NADH + H+ + ubiquinone = NAD+ + ubiquinol

• NADH_dehy_S2_C (PF06444 )
• Oxidored_q1 (PF00361 )

• 1-33

• 59-81
• 93-115
• 149-171
• 178-195
• 200-219
• 239-261
• 276-298
• 324-346

1. Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
2. Sanger F, Coulson AR, Barrell BG, Smith AJ, Roe BA: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161-78. [PubMed ]
3. Wise CA, Sraml M, Easteal S: Departure from neutrality at the mitochondrial NADH dehydrogenase subunit 2 gene in humans, but not in chimpanzees. Genetics. 1998 Jan;148(1):409-21. [PubMed ]
4. Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
5. Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
6. Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
7. Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
8. Johns DR, Berman J: Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1324-30. [PubMed ]
9. Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
10. Brown MD, Voljavec AS, Lott MT, Torroni A, Yang CC, Wallace DC: Mitochondrial DNA complex I and III mutations associated with Leber's hereditary optic neuropathy. Genetics. 1992 Jan;130(1):163-73. [PubMed ]
11. Lin FH, Lin R, Wisniewski HM, Hwang YW, Grundke-Iqbal I, Healy-Louie G, Iqbal K: Detection of point mutations in codon 331 of mitochondrial NADH dehydrogenase subunit 2 in Alzheimer's brains. Biochem Biophys Res Commun. 1992 Jan 15;182(1):238-46. [PubMed ]
12. Rieder MJ, Taylor SL, Tobe VO, Nickerson DA: Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome. Nucleic Acids Res. 1998 Feb 15;26(4):967-73. [PubMed ]

1. Pulmonary flavin-containing monooxygenase 2
2. FMO 2
3. Dimethylaniline oxidase 2
4. FMO 1B1

MAKKVAVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGVWRFKENVEDGRASIYQSVVT
NTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVLSVRKCPDFS
SSGQWKVVTQSNGKEQSAVFDAVMVCSGHHILPHIPLKSFPGMERFKGQYFHSRQYKHPD
GFEGKRILVIGMGNSGSDIAVELSKNAAQVFISTRHGTWVMSRISEDGYPWDSVFHTRFR
SMLRNVLPRTAVKWMIEQQMNRWFNHENYGLEPQNKYIMKEPVLNDDVPSRLLCGAIKVK
STVKELTETSAIFEDGTVEENIDVIIFATGYSFSFPFLEDSLVKVENNMVSLYKYIFPAH
LDKSTLACIGLIQPLGSIFPTAELQARWVTRVFKGLCSLPSERTMMMDIIKRNEKRIDLF
GESQSQTLQTNYVDYLDELALEIGAKPDFCSLLFKDPKLAVRLYFGPCNSYQYRLVGPGQ
WEGARNAIFTQKQRILKPLKTRALKDSSNFSVSFLLKILGLLAVVVAFFCQLQWS

• N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O

• FMO-like (PF00743 )

• None

• 510-532

ATGGCAAAGAAGGTAGCTGTGATTGGAGCTGGGGTCAGTGGCCTAATTTCTCTGAAGTGC
TGTGTGGATGAGGGACTTGAGCCCACTTGCTTTGAGAGAACTGAAGATATTGGAGGAGTG
TGGAGGTTCAAAGAGAATGTGGAAGATGGCCGAGCAAGTATCTATCAATCTGTCGTTACC
AACACCAGCAAAGAAATGTCCTGTTTCAGTGACTTTCCAATGCCTGAAGATTTTCCAAAC
TTCCTGCATAATTCTAAACTTCTGGAATATTTCAGGATTTTTGCTAAAAAATTTGATCTG
CTAAAATATATTCAGTTCCAGACAACTGTCCTTAGTGTGAGAAAATGTCCAGATTTCTCA
TCCTCTGGCCAATGGAAGGTTGTCACTCAGAGCAACGGCAAGGAGCAGAGTGCTGTCTTT
GACGCAGTTATGGTTTGCAGTGGCCACCACATTCTACCTCATATCCCACTGAAGTCATTT
CCAGGTATGGAGAGGTTCAAAGGCCAATATTTCCATAGCCGCCAATACAAGCATCCAGAT
GGATTTGAGGGAAAACGCATCCTGGTGATTGGAATGGGAAACTCAGGCTCAGATATTGCT
GTTGAGCTGAGTAAGAATGCTGCTCAGGTTTTTATCAGCACCAGGCATGGCACCTGGGTC
ATGAGCCGTATCTCTGAAGATGGCTATCCTTGGGACTCAGTGTTCCACACCCGGTTTCGT
TCTATGCTCCGCAATGTACTGCCACGAACAGCTGTAAAATGGATGATAGAACAACAGATG
AATCGGTGGTTCAACCATGAAAATTATGGCCTTGAGCCTCAAAACAAATACATTATGAAG
GAACCTGTACTAAATGATGATGTCCCAAGTCGTCTACTCTGTGGAGCCATCAAGGTGAAA
TCTACAGTGAAAGAGCTCACAGAAACTTCTGCCATCTTTGAGGATGGAACAGTGGAGGAG
AACATTGATGTCATCATTTTTGCAACAGGATATAGTTTCTCTTTTCCCTTCCTTGAAGAT
TCACTCGTTAAAGTAGAGAATAATATGGTCTCACTGTATAAATACATATTCCCCGCTCAC
CTGGACAAGTCAACCCTCGCGTGCATTGGTCTCATCCAGCCCCTAGGTTCCATTTTCCCA
ACTGCTGAACTTCAAGCTCGTTGGGTGACAAGAGTTTTCAAAGGCTTGTGTAGCCTGCCC
TCAGAGAGAACTATGATGATGGACATTATCAAAAGGAATGAAAAAAGAATTGACCTGTTT
GGAGAAAGCCAGAGCCAGACGTTGCAGACCAATTATGTTGACTACTTGGACGAGCTCGCC
TTAGAGATAGGTGCGAAGCCAGATTTCTGCTCTCTCTTGTTCAAAGATCCTAAACTGGCT
GTGAGACTCTATTTCGGACCCTGCAACTCCTATTAG

1. Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, Phillips IR: The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein. J Biol Chem. 1998 Nov 13;273(46):30599-607. [PubMed ]
2. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed ]

1. NADH-ubiquinone oxidoreductase subunit B14.5a
2. Complex I-B14.5a
3. CI-B14.5a

MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGR
RESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• CI-B14_5a (PF07347 )

• None

• None

ATGGCGTCCGCCACCCGTCTCATCCAGCGGCTGCGGAACTGGGCGTCCGGGCATGACCTG
CAGGGGAAGCTGCAGCTACGCTACCAGGAGATCTCCAAGCGAACTCAGCCTCCTCCCAAG
CTCCCTGTGGGTCCTAGCCACAAGCTCTCCAACAATTACTATTGCACTCGCGATGGCCGC
CGGGAATCTGTGCCCCCTTCCATCATCATGTCGTCGCAGAAGGCGCTGGTGTCAGGCAAG
CCAGCAGAGAGCTCTGCTGTAGCTGCCACTGAGAAGAAGGCGGTGACTCCAGCTCCTCCC
ATAAAGAGGTGGGAGCTGTCCTCGGACCAGCCTTACCTGTGA

1. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]
2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]

1. TR3
2. TR-beta
3. Selenoprotein Z
4. SelZ

MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQ
LGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQP
VPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLS
ADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI
GLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDST
TGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDV
VEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHG
QEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALG
IKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCCG

• Pyrimidine Metabolism (map00240 )

• thioredoxin + NADP+ = thioredoxin disulfide + NADPH + H+

• Pyr_redox (PF00070 )
• Pyr_redox_2 (PF07992 )
• Pyr_redox_dim (PF02852 )

• None

• None

ATGGCGGCAATGGCGGTGGCGCTGCGGGGATTAGGAGGGCGCTTCCGGTGGCGGACGCAG
GCCGTGGCGGGCGGGGTGCGGGGCGCGGCGCGGGGCGCAGCAGCAGGTCAGCGGGACTAT
GATCTCCTGGTGGTCGGCGGGGGATCTGGTGGCCTGGCTTGTGCCAAGGAGGCCGCCCAG
CTGGGAAGGAAGGTGGCCGTGGTGGACTACGTGGAACCTTCTCCCCAAGGCACCCGGTGG
GGCCTCGGCGGCACCTGCGTCAACGTGGGCTGCATCCCCAAGAAGCTGATGCACCAGGCG
GCACTGCTGGGAGGCCTGATCCAAGATGCCCCCAACTATGGCTGGGAGGTGGCCCAGCCC
GTGCCGCATGACTGGAGGAAGATGGCAGAAGCTGTTCAAAATCACGTGAAATCCTTGAAC
TGGGGCCACCGTGTCCAGCTTCAGGACAGAAAAGTCAAGTACTTTAACATCAAAGCCAGC
TTTGTTGACGAGCACACGGTTTGCGGCGTTGCCAAAGGTGGGAAAGAGATTCTGCTGTCA
GCCGATCACATCATCATTGCTACTGGAGGGCGGCCGAGATACCCCACGCACATCGAAGGT
GCCTTGGAATATGGAATCACAAGTGATGACATCTTCTGGCTGAAGGAATCCCCTGGAAAA
ACGTTGGTGGTCGGGGCCAGCTATGTGGCCCTGGAGTGTGCTGGCTTCCTCACCGGGATT
GGGCTGGACACCACCATCATGATGCGCAGCATCCCCCTCCGCGGCTTCGACCAGCAAATG
TCCTCCATGGTCATAGAGCACATGGCATCTCATGGCACCCGGTTCCTGAGGGGCTGTGCC
CCCTCGCGGGTCAGGAGGCTCCCTGATGGCCAGCTGCAGGTCACCTGGGAGGACAGCACC
ACCGGCAAGGAGGACACGGGCACCTTTGACACCGTCCTGTGGGCCATAGGTCGAGTCCCA
GACACCAGAAGTCTGAATTTGGAGAAGGCTGGGGTAGATACTAGCCCCGACACTCAGAAG
ATCCTGGTGGACTCCCGGGAAGCCACCTCTGTGCCCCACATCTACGCCATTGGTGACGTG
GTGGAGGGGCGGCCTGAGCTGACACCCATAGCGATCATGGCCGGGAGGCTCCTGGTGCAG
CGGCTCTTCGGCGGGTCCTCAGATCTGATGGACTACGACAATGTTCCCACGACCGTCTTC
ACCCCGCTGGAGTATGGCTGTGTGGGGCTGTCCGAGGAGGAGGCAGTGGCTCGCCACGGG
CAGGAGCATGTTGAGGTCTATCACGCCCATTATAAACCACTGGAGTTCACGGTGGCTGGA
CGAGATGCATCCCAGTGTTATGTAAAGATGGTGTGCCTGAGGGAGCCCCCACAGCTGGTG
CTGGGCCTGCATTTCCTTGGCCCCAACGCAGGCGAAGTTACTCAAGGATTTGCTCTGGGG
ATCAAGTGTGGGGCTTCCTATGCGCAGGTGATGCGGACCGTGGGTATCCATCCCACATGC
TCTGAGGAGGTAGTCAAGCTGCGCATCTCCAAGCGCTCAGGCCTGGACCCCACGGTGACA
GGCTGCTGAGGGTAA

1. Sun QA, Wu Y, Zappacosta F, Jeang KT, Lee BJ, Hatfield DL, Gladyshev VN: Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases. J Biol Chem. 1999 Aug 27;274(35):24522-30. [PubMed ]
2. Gasdaska PY, Berggren MM, Berry MJ, Powis G: Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett. 1999 Jan 8;442(1):105-11. [PubMed ]
3. Miranda-Vizuete A, Damdimopoulos AE, Pedrajas JR, Gustafsson JA, Spyrou G: Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization. Eur J Biochem. 1999 Apr;261(2):405-12. [PubMed ]
4. Lescure A, Gautheret D, Carbon P, Krol A: Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. [PubMed ]
5. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
6. Sun QA, Zappacosta F, Factor VM, Wirth PJ, Hatfield DL, Gladyshev VN: Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicing. J Biol Chem. 2001 Feb 2;276(5):3106-14. Epub 2000 Nov 1. [PubMed ]

1. NADH-ubiquinone oxidoreductase B8 subunit
2. Complex I-B8
3. CI-B8

MAAAAASRGVGAKLGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPILIRECSD
VQPKLWARYAFGQETNVPLNNFSADQVTRALENVLSGKA

• Oxidative phosphorylation (map00190 )

• NADH + H+ + acceptor = NAD+ + reduced acceptor

• L51_S25_CI-B8 (PF05047 )

• None

• None