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Human Metabolome Database Version 2.5

 

Showing metabocard for Succinic acid semialdehyde (HMDB01259)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:37
Accession Number HMDB01259
Secondary Accession Numbers Not Available
Common Name Succinic acid semialdehyde
Description Succinic acid semialdehyde is an intermediate in the catabolism of gamma-aminobutyrate (PMID 16435183). Succinate semialdehyde dehydrogenase is an enzyme that catalyses the reaction of succinate semialdehyde and NAD+ to form succinate and NADH. Succinic semialdehyde dehydrogenase (SSADH) deficiency (gamma-hydroxybutyric aciduria) is a rare neurometabolic disorder of gamma-aminobutyric acid degradation. Symptoms include motor delay, hypotonia, speech delay, autistic features, seizures, and ataxia. Patients also exhibit behavioral problems, such as attention deficit, hyperactivity, anxiety, or aggression. (PMID: 18622364)
Synonyms
  1. 2-formylpropionic acid ethyl ester
  2. 3-Formylpropanoate
  3. 3-Formylpropanoic acid
  4. 4-Oxobutanoate
  5. 4-Oxobutanoic acid
  6. Butryaldehydate
  7. Butryaldehydic acid
  8. Succinaldehydate
  9. Succinic acid semialdehyde
  10. Succinic semialdehyde
  11. beta-Formylpropionate
  12. beta-Formylpropionic acid
  13. gamma-Oxybutyrate
  14. gamma-Oxybutyric acid
  15. Succinate semialdehyde
Chemical IUPAC Name 4-oxobutanoic acid
Chemical Formula C4H6O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Keto-Acids
Sub Class
  • Short chain keto-acids
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • carboxylic acid
Biofunction
  • Component of Butanoate metabolism
  • Component of Glutamate metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 102.089
Monoisotopic Molecular Weight 102.031693
Isomeric SMILES OC(=O)CCC=O
Canonical SMILES OC(=O)CCC=O
KEGG Compound ID C00232 Link Image
BioCyc ID SUCC-S-ALD Link Image
BiGG ID 34331 Link Image
Wikipedia Link Succinic semialdehyde Link Image
NuGOwiki Link HMDB01259 Link Image
Metagene Link HMDB01259 Link Image
METLIN ID 6114 Link Image
PubChem Compound 1112 Link Image
PubChem Substance 3190 Link Image
ChEBI ID 16265 Link Image
CAS Registry Number 692-29-5
InChI Identifier InChI=1/C4H6O3/c5-3-1-2-4(6)7/h3H,1-2H2,(H,6,7)
Synthesis Reference Bruce, R.; Sims, K.; Pitts, F. N., Jr. Synthesis and purification of succinic semialdehyde. Analytical Biochemistry (1971), 41(1), 271-3.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 654.0 mg/mL [MEYLAN,WM et al. (1996)]; 194.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.47 [Predicted by ALOGPS]; -0.3 [Predicted by PubChem via XLOGP]; -0.42 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • mitochondria
Biofluid Location
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Testes —
Concentrations (Normal)
Biofluid CSF
Value 28.5 (24.0-33.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Urine
Value 0.35 (0.14-0.54) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 0.39 (0.28-0.51) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
General References
  1. Du L, Musson DG, Wang AQ: Stability studies of vorinostat and its two metabolites in human plasma, serum and urine. J Pharm Biomed Anal. 2006 Nov 16;42(5):556-64. Epub 2006 Jul 5. [PubMed Link Image]
  2. Du L, Musson DG, Wang AQ: High turbulence liquid chromatography online extraction and tandem mass spectrometry for the simultaneous determination of suberoylanilide hydroxamic acid and its two metabolites in human serum. Rapid Commun Mass Spectrom. 2005;19(13):1779-87. [PubMed Link Image]
  3. Hinshelwood A, McGarvie G, Ellis EM: Substrate specificity of mouse aldo-keto reductase AKR7A5. Chem Biol Interact. 2003 Feb 1;143-144:263-9. [PubMed Link Image]
  4. Lee BC, Choe YS, Chi DY, Paik JY, Lee KH, Choi Y, Kim BT: 8-cyclopentadienyltricarbonyl 99mtc 8-oxooctanoic acid: a novel radiotracer for evaluation of medium chain fatty acid metabolism in the liver. Bioconjug Chem. 2004 Jan-Feb;15(1):121-7. [PubMed Link Image]
  5. Parise RA, Holleran JL, Beumer JH, Ramalingam S, Egorin MJ: A liquid chromatography-electrospray ionization tandem mass spectrometric assay for quantitation of the histone deacetylase inhibitor, vorinostat (suberoylanilide hydroxamicacid, SAHA), and its metabolites in human serum. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Aug 18;840(2):108-15. Epub 2006 May 24. [PubMed Link Image]
  6. Wikipedia Link Image
Metabolic Enzymes
  1. 4-aminobutyrate aminotransferase, mitochondrial precursor
  2. Succinate semialdehyde dehydrogenase, mitochondrial precursor
  3. Alcohol dehydrogenase iron-containing 1
  4. cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
Enzyme 1 [top]
Enzyme 1 ID 5480
Enzyme 1 Name 4-aminobutyrate aminotransferase, mitochondrial precursor
Enzyme 1 Synonyms
  1. (S-3-amino-2-methylpropionate transaminase
  2. Gamma-amino-N-butyrate transaminase
  3. GABA transaminase
  4. GABA aminotransferase
  5. GABA-AT
  6. GABA-T
  7. L-AIBAT
Enzyme 1 Gene Name ABAT
Enzyme 1 Protein Sequence >4-aminobutyrate aminotransferase, mitochondrial precursor 
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Enzyme 1 Number of Residues 500
Enzyme 1 Molecular Weight 56440
Enzyme 1 Theoretical pI 8.04
Enzyme 1 GO Classification
Function
  • 4-aminobutyrate transaminase activity
  • binding
  • catalytic activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
  • amino acid and derivative metabolism
  • amino acid derivative metabolism
  • cellular metabolism
  • gamma-aminobutyric acid metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine
Enzyme 1 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 602705 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P80404 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GABT_HUMAN Link Image
Enzyme 1 PDB ID 1OHY Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1503 bp 
ATGGCCTCCATGTTGCTCGCCCAGCGGCTGGCCTGCAGCTTCCAGCACACGTACCGCCTG
CTGGTGCCTGGATCCAGACACATTAGTCAAGCTGCAGCCAAAGTCGACGTTGAATTTGAT
TATGATGGGCCTCTGATGAAGACGGAAGTCCCAGGGCCTAGATCTCAGGAGTTAATGAAA
CAGCTGAATATAATTCAGAATGCAGAGGCTGTGCATTTTTTCTGCAATTACGAAGAGAGC
CGAGGCAATTACCTGGTTGATGTGGACGGCAACCGAATGCTGGATCTTTATTCCCAGATC
TCCTCTGTTCCCATAGGTTACAGCGACCCGGCCCTCGTGAAACTCATCCAACAGCCACAA
AATGCGAGCATGTTTGTCAACAGACCCGCCCTCGAAATCCTGCCTCCGGAGAACTTTGTG
GAGAAGCTCCGGCAGTCCTTGCTCTCGGTGGCTCCCAAAGGGATGTCCCAGCTCATCACC
ATGGCCTGCGGCTCCTGCTCCAATGAAAACGCCTTAAAGACCATCTTCATGTGGTACCGG
AGCAAGGAAAGAGGGCAGAGGGGATTCTCCAAAGAGGAGCTGGAGACGTGCATGATTAAC
CAGGCCCCCTGGTGCCCCGACTACAGCATCCTCTCCTTCATGGGTTCCTTCCATGGGAGG
ACCATGGGTTGCTTAGCGACCACGCACTCTAAAGCCATTCACAAGATCGATATCCCTTCC
TTTGACTGGCCCATCGCACCGTTCCCACGGCTGAAATACCCTCTGGAAGAGTTTGTGAAA
GAGAACCAACAGGAAGAGGCCGGCTGTCTGGAAGAGGTTGAGGATCTGATTGTGAAATAT
CGAAAAAAGAAGAAGACGGTGGCCGGGATCATCGTGGAGCCCATCCAGTCCGAGGGTGGA
GACAACCATGCATCCGATGACTTCTTTCGGAAGCTGAGAGACATCGCCAGGAAGCACTGC
TGCGCCTTCTTGGTGGACGAGGTCCAGACCGGAGGAGGCTGCACGGGCAAGTTCTGGGCC
CATGAGCACTGGGGCCTGGATGACCCAGCAGACGTGATGACCTTCAGCAAGAAGATGATG
ACTGGGGGCTTCTTCCTCAAGGAGGAGTTCAGGCCTAATGCTCCCTACCGGATCTTCAAC
ACGTGGCTGGGGGACCCGTCCAAGAACCTGTTGCTGGCTGAGGTCATCAACATCATCAAG
CGGGAGGACCTGCTAAATAATGCAGCCCATGCCGGGAAGGCCCTGCTCACAGGACTGCTG
GACCTCCAGGCCCGGTACCCCCAGTTCATCAGCAGGGTGAGAGGACGAGGCACCTTTTGC
TCCTTCGATACTCCCGATGATTCCATACGGAATAAGCTCATTTTAATTGCCAGAAACAAA
GGTGTGGTGTTGGGTGGCTGTGGTGACAAATCCATTCGTTTCCGTCCCACGCTGGTGTTC
AGGGATCACCACGCTCACCTGTTCCTCAATATTTTCAGTGACATCTTAGCAGACTTCAAG
TAA
Enzyme 1 GenBank Gene ID L32961 Link Image
Enzyme 1 GeneCard ID ABAT Link Image
Enzyme 1 GenAtlas ID ABAT Link Image
Enzyme 1 HGNC ID HGNC:23 Link Image
Enzyme 1 Chromosome Location 16
Enzyme 1 Locus 16p13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Osei YD, Churchich JE: Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase. Gene. 1995 Apr 3;155(2):185-7. [PubMed Link Image]
  2. De Biase D, Barra D, Simmaco M, John RA, Bossa F: Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur J Biochem. 1995 Jan 15;227(1-2):476-80. [PubMed Link Image]
  3. Medina-Kauwe LK, Tobin AJ, De Meirleir L, Jaeken J, Jakobs C, Nyhan WL, Gibson KM: 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. J Inherit Metab Dis. 1999 Jun;22(4):414-27. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5481
Enzyme 2 Name Succinate semialdehyde dehydrogenase, mitochondrial precursor
Enzyme 2 Synonyms
  1. NAD(+-dependent succinic semialdehyde dehydrogenase
Enzyme 2 Gene Name ALDH5A1
Enzyme 2 Protein Sequence >Succinate semialdehyde dehydrogenase, mitochondrial precursor 
MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLR
TDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKER
SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIH
TPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALAL
AELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSV
KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAF
AEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFF
EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWR
VAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
Enzyme 2 Number of Residues 535
Enzyme 2 Molecular Weight 57215
Enzyme 2 Theoretical pI 8.37
Enzyme 2 GO Classification
Function
  • aldehyde dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH
Enzyme 2 Pathways
Enzyme 2 Reactions
  • succinate semialdehyde + NAD+ + H2O = succinate + NADH + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 3766467 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P51649 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SSDH_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1608 bp 
ATGGCGACCTGCATTTGGCTGCGGAGCTGTGGGGCCCGGCGCCTCGGGTCGACGTTTCCA
GGCTGCCGCCTCCGCCCCCGCGCCGGCGGCCTGGTCCCTGCCTCCGGGCCTGCGCCCGGC
CCGGCCCAGCTCCGCTGCTACGCTGGGCGCCTGGCGGGCCTCTCTGCGGCGCTGCTGCGC
ACCGACAGCTTCGTGGGCGGCCGCTGGCTCCCGGCCGCCGCCACCTTCCCCGTGCAAGAC
CCGGCCAGCGGCGCCGCTCTGGGCATGGTAGCCGACTGCGGGGTGCGAGAGGCCCGCGCC
GCCGTGCGCGCTGCCTACGAGGCTTTCTGCCGCTGGAGGGAGGTCTCCGCCAAGGAGAGG
AGTTCATTACTTCGGAAGTGGTACAATTTAATGATACAAAATAAGGATGACCTTGCCAGA
ATAATCACAGCTGAAAGTGGAAAGCCACTGAAGGAGGCACATGGAGAAATTCTCTATTCC
GCCTTTTTCCTAGAGTGGTTCTCTGAGGAAGCCCGCCGTGTTTACGGAGACATTATCCAC
ACCCCGGCAAAGGACAGGCGGGCCCTGGTCCTCAAGCAGCCCATAGGCGTGGCTGCAGTC
ATCACCCCGTGGAATTTCCCCAGTGCCATGATCACCCGGAAGGTGGGGGCCGCCCTGGCA
GCCGGCTGTACTGTCGTGGTGAAGCCTGCCGAAGACACGCCCTTCTCCGCCCTGGCCCTG
GCTGAGCTTGCAAGCCAGGCTGGGATTCCTTCAGGTGTATACAATGTTATTCCCTGTTCT
CGAAAGAATGCCAAGGAAGTAGGGGAGGCAATTTGTACTGATCCTCTGGTGTCCAAAATT
TCCTTTACTGGTTCAACAACTACAGGAAAGATCCTGTTGCACCACGCAGCAAACTCTGTG
AAAAGGGTCTCTATGGAGCTGGGCGGCCTTGCTCCATTTATAGTATTTGACAGTGCCAAC
GTGGACCAGGCTGTAGCAGGGGCCATGGCATCTAAATTTAGGAACACTGGACAGACTTGT
GTTTGCTCAAACCAATTCTTGGTGCAAAGGGGCATCCATGATGCCTTTGTAAAAGCATTC
GCCGAGGCCATGAAGAAGAACCTGCGCGTAGGTAATGGATTTGAGGAAGGAACTACTCAG
GGCCCATTAATTAATGAAAAAGCGGTAGAAAAGGTGGAGAAACAGGTGAATGATGCCGTT
TCTAAAGGTGCCACCGTTGTGACAGGTGGAAAACGACACCAACTTGGAAAAAATTTCTTT
GAGCCTACCCTGCTGTGCAATGTCACCCAGGACATGCTGTGCACTCATGAAGAGACTTTC
GGGCCTCTGGCACCAGTTATCAAGTTCGATACAGAGGAGGAGGCTATAGCAATCGCTAAC
GCAGCTGATGTTGGGTTAGCAGGTTATTTTTACTCTCAAGACCCAGCCCAGATCTGGAGA
GTGGCAGAGCAGCTGGAAGTGGGCATGGTTGGCGTCAACGAAGGATTAATTTCCTCTGTG
GAGTGCCCTTTTGGTGGAGTGAAGCAGTCCGGCCTTGGGCGAGAGGGGTCCAAGTATGGC
ATTGATGAGTATCTGGAACTCAAGTATGTGTGTTACGGGGGCTTGTAG
Enzyme 2 GenBank Gene ID Y11192 Link Image
Enzyme 2 GeneCard ID ALDH5A1 Link Image
Enzyme 2 GenAtlas ID ALDH5A1 Link Image
Enzyme 2 HGNC ID HGNC:408 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6p22.2-p22.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Chambliss KL, Hinson DD, Trettel F, Malaspina P, Novelletto A, Jakobs C, Gibson KM: Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria). Am J Hum Genet. 1998 Aug;63(2):399-408. [PubMed Link Image]
  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 Link Image]
  3. Chambliss KL, Caudle DL, Hinson DD, Moomaw CR, Slaughter CA, Jakobs C, Gibson KM: Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression. J Biol Chem. 1995 Jan 6;270(1):461-7. [PubMed Link Image]
  4. Trettel F, Malaspina P, Jodice C, Novelletto A, Slaughter CA, Caudle DL, Hinson DD, Chambliss KL, Gibson KM: Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization. Adv Exp Med Biol. 1997;414:253-60. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 9419
Enzyme 3 Name Alcohol dehydrogenase iron-containing 1
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name ADHFE1
Enzyme 3 Protein Sequence >Alcohol dehydrogenase iron-containing 1 
MAAAARARVAYLLRQLQRAACQCPTHSHTYSQAPGLSPSGKTTDYAFEMAVSNIRYGAAV
TKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFM
EAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKP
LIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSG
FDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRN
PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLS
VVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGL
AAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASMKLY
Enzyme 3 Number of Residues 467
Enzyme 3 Molecular Weight 50308
Enzyme 3 Theoretical pI Not Available
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Energy production and conversion
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • 3,4-Dihydroxymandelaldehyde + H+ + Nicotinamide adenine dinucleotide - reduced <==> 3,4-Dihydroxyphenylethyleneglycol + Nicotinamide adenine dinucleotide
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 25989126 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8IWW8 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q8IWW8_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AY033237 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID ADHFE1 Link Image
Enzyme 3 HGNC ID HGNC:16354 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Deng Y, Wang Z, Gu S, Ji C, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1). DNA Seq. 2002 Oct;13(5):301-6. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 12979
Enzyme 4 Name cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase
Enzyme 4 Synonyms
  1. ABAT, nuclear gene encoding mitochondrial protein, transcript variant 2, mRNA
Enzyme 4 Gene Name Not Available
Enzyme 4 Protein Sequence >cDNA FLJ75643, highly similar to Homo sapiens 4-aminobutyrate aminotransferase 
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
Enzyme 4 Number of Residues 500
Enzyme 4 Molecular Weight 56440
Enzyme 4 Theoretical pI 8.04
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 158254434 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A8K386 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A8K386_HUMAN Link Image
Enzyme 4 PDB ID 1OHY Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK290501 Link Image
Enzyme 4 GeneCard ID A8K386 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs Not Available
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available