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Enzyme 1
[top]
|
| Enzyme 1 ID |
5447 |
| Enzyme 1 Name |
Hexokinase-1 |
| Enzyme 1 Synonyms |
- Brain form hexokinase
- Hexokinase type I
- HK I
|
| Enzyme 1 Gene Name |
HK1 |
| Enzyme 1 Protein Sequence |
>Hexokinase-1
MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTAT
VKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVH
GSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGV
EGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME
ELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGM
YLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLG
VEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTH
PQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLT
KDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRV
LLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGF
TFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVG
TMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDD
IRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRG
IFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAA
VVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKG
AALITAVGVRLRTEASS
|
| Enzyme 1 Number of Residues |
917 |
| Enzyme 1 Molecular Weight |
102485.1 |
| Enzyme 1 Theoretical pI |
6.78 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hexokinase activity
- nucleoside binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in ATP binding |
| Enzyme 1 Specific Function |
ATP + D-hexose = ADP + D-hexose 6-phosphate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + D-hexose = ADP + D-hexose 6-phosphate [RN:R02848]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
184021  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P19367  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
HXK1_HUMAN  |
| Enzyme 1 PDB ID |
1HKB  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>2754 bp
ATGATCGCCGCGCAGCTCCTGGCCTATTACTTCACGGAGCTGAAGGATGACCAGGTCAAA
AAGATTGACAAGTATCTGTATGCCATGCGGCTCTCCGATGAAACTCTCATAGATATCATG
ACTCGCTTCAGGAAGGAGATGAAGAATGGCCTCTCCCGGGATTTTAATCCAACAGCCACA
GTCAAGATGTTGCCAACATTCGTAAGGTCCATTCCTGATGGCTCTGAAAAGGGAGATTTC
ATTGCCCTGGATCTTGGTGGGTCTTCCTTTCGAATTCTGCGGGTGCAAGTGAATCATGAG
AAAAACCAGAATGTTCACATGGAGTCCGAGGTTTATGACACCCCAGAGAACATCGTGCAC
GGCAGTGGAAGCCAGCTTTTTGATCATGTTGCTGAGTGCCTGGGAGATTTCATGGAGAAA
AGGAAGATCAAGGACAAGAAGTTACCTGTGGGATTCACGTTTTCTTTTCCTTGCCAACAA
TCCAAAATAGATGAGGCCATCCTGATCACCTGGACAAAGCGATTTAAAGCGAGCGGAGTG
GAAGGAGCAGATGTGGTCAAACTGCTTAACAAAGCCATCAAAAAGCGAGGGGACTATGAT
GCCAACATCGTAGCTGTGGTGAATGACACAGTGGGCACCATGATGACCTGTGGCTATGAC
GACCAGCACTGTGAAGTCGGCCTGATCATCGGCACTGGCACCAATGCTTGCTACATGGAG
GAACTGAGGCACATTGATCTGGTGGAAGGAGACGAGGGGAGGATGTGTATCAATACAGAA
TGGGGAGCCTTTGGAGACGATGGATCATTAGAAGACATCCGGACAGAGTTTGACAGGGAG
ATAGACCGGGGATCCCTCAACCCTGGAAAACAGCTGTTTGAGAAGATGGTCAGTGGCATG
TACTTGGGAGAGCTGGTTCGACTGATCCTAGTCAAGATGGCCAAGGAGGGCCTCTTATTT
GAAGGGCGGATCACCCCGGAGCTGCTCACCCGAGGGAAGTTTAACACCAGTGATGTGTCA
GCCATCGAAAAGAATAAGGAAGGCCTCCACAATGCCAAAGAAATCCTGACCCGCCTGGGA
GTGGAGCCGTCCGATGATGACTGTGTCTCAGTCCAGCACGTTTGCACCATTGTCTCATTT
CGCTCAGCCAACTTGGTGGCTGCCACACTGGGCGCCATCTTGAACCGCCTGCGTGATAAC
AAGGGCACACCCAGGCTGCGGACCACGGTTGGTGTCGACGGATCTCTTTACAAGACGCAC
CCACAGTATTCCCGGCGTTTCCACAAGACTCTAAGGCGCTTGGTGCCAGACTCCGATGTG
CGCTTCCTCCTCTCGGAGAGTGGCAGCGGCAAGGGGGCTGCCATGGTGACGGCGGTGGCC
TACCGCTTGGCCGAGCAGCACCGGCAGATAGAGGAGACCCTGGCTCATTTCCACCTCACC
AAAGACATGCTGCTGGAGGTGAAGAAGAGGATGCGGGCCGAGATGGAGCTGGGGCTGAGG
AAGCAGACGCACAACAATGCCGTGGTTAAGATGCTGCCCTCCTTCGTCCGGAGAACTCCC
GACGGGACCGAGAATGGTGACTTCTTGGCCCTGGATCTTGGAGGAACCAATTTCCGTGTG
CTGCTGGTGAAAATCCGTAGTGGGAAAAAGAGAACGGTGGAAATGCACAACAAGATCTAC
GCCATTCCTATTGAAATCATGCAGGGCACTGGGGAAGAGCTGTTTGATCACATTGTCTCC
TGCATCTCTGACTTCTTGGACTACATGGGGATCAAAGGCCCCAGGATGCCTCTGGGCTTC
ACGTTCTCATTTCCCTGCCAGCAGACGAGTCTGGACGCGGGAATCTTGATCACGTGGACA
AAGGGTTTTAAGGCAACAGACTGCGTGGGCCACGATGTAGTCACCTTACTAAGGGATGCG
ATAAAAAGGAGAGAGGAATTTGACCTGGACGTGGTGGCTGTGGTCAACGACACAGTGGGC
ACCATGATGACCTGTGCTTATGAGGAGCCCACCTGTGAGGTTGGACTCATTGTTGGGACC
GGCAGCAATGCCTGCTACATGGAGGAGATGAAGAACGTGGAGATGGTGGAGGGGGACCAG
GGGCAGATGTGCATCAACATGGAGTGGGGGGCCTTTGGGGACAACGGGTGTCTGGATGAT
ATCAGGACACACTACGACAGACTGGTGAACGAATATTCCCTAAATGCTGGGAAACAAAGG
TATGAGAAGATGATCAGTGGTATGTACCTGGGTGAAATCGTCCGCAACATCTTAATCGAC
TTCACCAAGAAGGGATTCCTCTTCCGAGGGCAGATCTCTGAGACGATGAAGACCCGGGGC
ATCTTTGAGACCAAGTTTCTCTCTCAGATCGAGAGTGACCGATTAGCACTGCTCCAGGTC
CGGGCTATCCTCCAGCAGCTAGGTCTGAATAGCACCTGCGATGACAGTATCCTCGTCAAG
ACAGTGTGCGGGGTGGTGTCCAGGAGGGCCGCACAGCTGTGTGGCGCAGGCATGGCTGCG
GTTGTGGATAAGATCCGCGAGAACAGAGGACTGGACCGTCTGAATGTGACTGTGGGAGTG
GACGGGACACTCTACAAGCTTCATCCACACTTCTCCAGAATCATGCACCAGACGGTGAAG
GAACTGTCACCAAAATGTAACGTGTCCTTCCTCCTGTCTGAGGATGGCAGCGGCAAGGGG
GCCGCCCTCATCACGGCCGTGGGCGTGCGGTTACGCACAGAGGCAAGCAGCTAA
|
| Enzyme 1 GenBank Gene ID |
M75126  |
| Enzyme 1 GeneCard ID |
HK1  |
| Enzyme 1 GenAtlas ID |
HK1  |
| Enzyme 1 HGNC ID |
HGNC:4922  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
10q22 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Nishi S, Seino S, Bell GI: Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous. Biochem Biophys Res Commun. 1988 Dec 30;157(3):937-43. [PubMed
]
- Ruzzo A, Andreoni F, Magnani M: Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region. Biochem J. 1998 Apr 15;331 ( Pt 2):607-13. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Andreoni F, Ruzzo A, Magnani M: Structure of the 5' region of the human hexokinase type I (HKI) gene and identification of an additional testis-specific HKI mRNA. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):19-26. [PubMed
]
- Magnani M, Serafini G, Bianchi M, Casabianca A, Stocchi V: Human hexokinase type I microheterogeneity is due to different amino-terminal sequences. J Biol Chem. 1991 Jan 5;266(1):502-5. [PubMed
]
- Magnani M, Bianchi M, Casabianca A, Stocchi V, Daniele A, Altruda F, Ferrone M, Silengo L: A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates. Biochem J. 1992 Jul 1;285 ( Pt 1):193-9. [PubMed
]
- Murakami K, Piomelli S: Identification of the cDNA for human red blood cell-specific hexokinase isozyme. Blood. 1997 Feb 1;89(3):762-6. [PubMed
]
- Aleshin AE, Zeng C, Fromm HJ, Honzatko RB: Crystallization and preliminary X-ray analysis of human brain hexokinase. FEBS Lett. 1996 Aug 5;391(1-2):9-10. [PubMed
]
- Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. Structure. 1998 Jan 15;6(1):39-50. [PubMed
]
- Aleshin AE, Zeng C, Bartunik HD, Fromm HJ, Honzatko RB: Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate. J Mol Biol. 1998 Sep 18;282(2):345-57. [PubMed
]
- Rosano C, Sabini E, Rizzi M, Deriu D, Murshudov G, Bianchi M, Serafini G, Magnani M, Bolognesi M: Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control. Structure. 1999 Nov 15;7(11):1427-37. [PubMed
]
- Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. J Mol Biol. 2000 Mar 3;296(4):1001-15. [PubMed
]
- Bianchi M, Magnani M: Hexokinase mutations that produce nonspherocytic hemolytic anemia. Blood Cells Mol Dis. 1995;21(1):2-8. [PubMed
]
- van Wijk R, Rijksen G, Huizinga EG, Nieuwenhuis HK, van Solinge WW: HK Utrecht: missense mutation in the active site of human hexokinase associated with hexokinase deficiency and severe nonspherocytic hemolytic anemia. Blood. 2003 Jan 1;101(1):345-7. Epub 2002 Aug 8. [PubMed
]
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| Enzyme 1 Metabolite References |
Not Available |
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Enzyme 2
[top]
|
| Enzyme 2 ID |
5523 |
| Enzyme 2 Name |
Sucrase-isomaltase, intestinal |
| Enzyme 2 Synonyms |
- Sucrase
- Isomaltase
|
| Enzyme 2 Gene Name |
SI |
| Enzyme 2 Protein Sequence |
>Sucrase-isomaltase, intestinal
MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDS
GKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMT
TTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEF
TGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISARLPSDYIYG
IGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSN
AMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRW
NYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQ
KYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNP
NCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMY
SKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAH
WLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSR
NHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHE
FYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDM
YLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDT
IQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMN
AHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGC
VWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRV
EVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRS
SGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPP
GYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGP
TPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDI
DYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVF
VKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVD
FYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEA
EQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGD
NYARWDNMDKSIIGMMEFSLFGISYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNI
ANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKP
TWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDT
INLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLY
LSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNE
DTTNMILRIDLTTHNVTLEEPIEINWS
|
| Enzyme 2 Number of Residues |
1827 |
| Enzyme 2 Molecular Weight |
209403.4 |
| Enzyme 2 Theoretical pI |
5.35 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in catalytic activity |
| Enzyme 2 Specific Function |
Plays an important role in the final stage of carbohydrate digestion |
| Enzyme 2 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 2 Reactions |
- Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action [RN:R00801 R06087] ALL_REAC R00801 R06087(G) > R00802 R06088(G)
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
36645  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P14410  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SUIS_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>5484 bp
ATGGCAAGAAAGAAATTTAGTGGATTGGAAATCTCTCTGATTGTCCTTTTTGTCATAGTT
ACTATAATAGCTATTGCCTTAATTGTTGTTTTAGCAACTAAGACACCTGCTGTTGATGAA
ATTAGTGATTCTACTTCAACTCCAGCTACTACTCGTGTGACTACAAATCCTTCTGATTCA
GGAAAATGTCCAAATGTGTTAAATGATCCTGTCAATGTGAGAATAAACTGCATTCCAGAA
CAATTCCCAACAGAGGGAATTTGTGCACAGAGAGGCTGCTGCTGGAGGCCGTGGAATGAC
TCTCTTATTCCTTGGTGCTTCTTCGTTGATAATCATGGTTATAACGTTCAAGACATGACA
ACAACAAGTATTGGAGTTGAAGCCAAATTAAACAGGATACCTTCACCTACACTATTTGGA
AATGACATCAACAGTGTTCTCTTCACAACTCAAAATCAGACACCCAATCGTTTCCGGTTC
AAGATTACTGATCCAAATAATAGAAGATATGAAGTTCCTCATCAGTATGTAAAAGAGTTT
ACTGGACCCACAGTTTCTGATACGTTGTATGATGTGAAGGTTGCCCAAAACCCATTTAGC
ATCCAAGTTATTAGGAAAAGCAACGGTAAAACTTTGTTTGACACCAGCATTGGTCCCTTA
GTGTACTCTGACCAGTACTTACAGATCTCAGCCCGTCTTCCAAGTGATTATATTTATGGT
ATTGGAGAACAAGTTCATAAGAGATTTCGTCATGATTTATCCTGGAAAACATGGCCAATT
TTTACTCGAGACCAACTTCCTGGTGATAATAATAATAATTTATACGGCCATCAAACATTC
TTTATGTGTATTGAAGATACATCTGGAAAGTCATTCGGTGTTTTTTTAATGAATAGCAAT
GCAATGGAGATTTTTATCCAGCCTACTCCAATAGTAACATATAGAGTTACCGGTGGCATT
CTGGATTTTTACATCCTTCTAGGAGATACACCAGAACAAGTAGTTCAACAGTATCAACAG
CTTGTTGGACTACCAGCAATGCCAGCATATTGGAATCTTGGATTCCAACTAAGTCGCTGG
AATTATAAGTCACTAGATGTAGTGAAAGAAGTGGTAAGGAGAAACCGGGAAGCTGGCATA
CCATTTGATACACAGGTCACTGATATTGACTACATGGAAGACAAGAAAGACTTTACTTAT
GATCAAGTTGCGTTTAACGGACTCCCTCAATTTGTGCAAGATTTGCATGACCATGGACAG
AAATATGTCATCATCTTGGACCCTGCAATTTCCATAGGTCGACGTGCCAATGGAACAACA
TATGCAACCTATGAGAGGGGAAACACACAACATGTGTGGATAAATGAGTCAGATGGAAGT
ACACCAATTATTGGAGAGGTATGGCCAGGATTAACAGTATACCCTGATTTCACTAATCCA
AACTGCATTGATTGGTGGGCAAATGAATGCAGTATTTTCCATCAAGAAGTGCAATATGAT
GGACTTTGGATTGACATGAATGAAGTTTCCAGCTTTATTCAAGGTTCAACAAAAGGATGT
AATGTAAACAAATTGAATTATCCACCGTTTACTCCTGATATTCTTGACAAACTCATGTAT
TCCAAAACAATTTGCATGGATGCTGTGCAGAACTGGGGTAAACAGTATGATGTTCATAGC
CTCTATGGATACAGCATGGCTATAGCCACAGAGCAAGCTGTACAAAAAGTTTTTCCTAAT
AAGAGAAGCTTCATTCTTACCCGCTCAACATTTGCTGGATCTGGAAGACATGCTGCTCAT
TGGTTAGGAGACAATACTGCTTCATGGGAACAAATGGAATGGTCTATAACTGGAATGCTG
GAGTTCAGTTTGTTTGGAATACCTTTGGTTGGAGCAGACATCTGTGGATTTGTGGCTGAA
ACCACAGAAGAACTTTGCAGAAGATGGATGCAACTTGGGGCATTTTATCCATTTTCCAGA
AACCATAATTCTGACGGATATGAACATCAGGATCCTGCATTTTTTGGGCAGAATTCACTT
TTGGTTAAATCATCAAGGCAGTATTTAACTATTCGCTACACCTTATTACCCTTCCTCTAC
ACTCTGTTTTATAAAGCCCATGTGTTTGGAGAAACAGTAGCAAGACCAGTTCTTCATGAG
TTTTATGAGGATACGAACAGCTGGATTGAGGACACTGAGTTTTTGTGGGGCCCTGCATTA
CTTATTACTCCTGTTCTAAAACAGGGAGCAGATACTGTGAGTGCCTACATCCCTGATGCT
ATTTGGTATGATTATGAATCTGGTGCAAAAAGGCCATGGAGGAAACAACGGGTTGATATG
TATCTTCCAGCAGACAAAATAGGATTACATCTTAGAGGAGGTTATATCATCCCCATTCAA
GAACCAGATGTAACAACAACAGCAAGCCGTAAGAATCCTCTAGGACTTATAGTCGCATTA
GGTGAAAACAACACAGCCAAAGGAGACTTTTTCTGGGATGATGGAGAAACTAAAGATACA
ATACAAAATGGCAACTACATATTATATACATTTTCAGTTTCTAATAACACATTAGATATT
GTGTGCACACATTCATCATATCAGGAAGGAACTACCTTAGCATTTCAGACTGTAAAAATC
CTTGGGTTGACAGACAGTGTTACAGAAGTTAGAGTGGCGGAAAATAATCAACCAATGAAC
GCTCATTCCAATTTCACTTATGATGCTTCTAACCAGGTTCTCCTAATTGCAGATCTCAAA
CTTAATCTTGGAAGAAACTTTAGTGTTCAATGGAATCAAATTTTCTCAGAAAATGAAAGA
TTTAATTGTTATCCAGATGCAGATTTGGCAACTGAACAAAAGTGCACACAACGTGGCTGT
GTATGGAGAACGGGTTCTTCTCTATCCAAAGCACCTGAGTGTTACTTTCCCAGACAAGAT
AACTCTTATTCAGTCAACTCAGCTCGCTATTCATCCATGGGTATAACAGCTGACCTCCAA
CTAAATACTGCAAATGCCAGAATAAAGTTACCTTCTGACCCCATCTCAACTCTTCGTGTG
GAGGTGAAATATCACAAAAATGATATGTTGCAGTTTAAGATTTATGATCCCCAAAAGAAG
AGATATGAAGTACCAGTACCGTTAAACATTCCAACCACCCCAATAAGTACTTATGAAGAC
AGACTTTATGATGTGGAAATCAAGGAAAATCCTTTTGGCATCCAGATTCGACGGAGAAGC
AGTGGAAGAGTCATTTGGGATTCTTGGCTGCCTGGATTTGCTTTTAATGACCAGTTCATT
CAAATATCGACTCGCCTGCCATCAGAATATATATATGGTTTTGGGGAAGTGGAACATACA
GCATTTAAGCGAGATCTGAACTGGAATACTTGGGGAATGTTCACAAGAGACCAACCCCCT
GGTTACAAACTTAATTCCTATGGATTTCATCCCTATTACATGGCTCTGGAAGAGGAGGGC
AATGCTCATGGTGTTTTCTTACTCAACAGCAATGCAATGGATGTTACATTCCAGCCAACT
CCTGCTCTAACTTACCGTACAGTTGGAGGGATCTTGGATTTTTATATGTTTTTGGGCCCA
ACTCCACAAGTTGCAACAAAGCAATACCATGAAGTAATTGGCCATCCAGTCATGCCAGCT
TATTGGGCTTTGGGATTCCAATTATGTCGTTATGGATATGCAAATACTTCAGAGGTTCGG
GAATTATATGACGCTATGGTGGCTGCTAACATCCCCTATGATGTTCAGTACACAGACATT
GACTACATGGAAAGGCAGCTAGACTTTACAATTGGTGAAGCATTCCAGGACCTTCCTCAG
TTTGTTGACAAAATAAGAGGAGAAGGAATGAGATACATTATTATCCTGGATCCAGCAATT
TCAGGAAATGAAACAAAGACTTACCCTGCATTTGAAAGAGGACAGCAGAATGATGTCTTT
GTCAAATGGCCAAACACCAATGACATTTGTTGGGCAAAGGTTTGGCCAGATTTGCCCAAC
ATAACAATAGATAAAACTCTAACGGAAGATGAAGCTGTTAATGCTTCCAGAGCTCATGTA
GCTTTCCCAGATTTCTTCAGGACTTCCACAGCAGAGTGGTGGGCCAGAGAAATTGTGGAC
TTTTACAATGAAAAGATGAAGTTTGATGGTTTGTGGATTGATATGAATGAGCCATCAAGT
TTTGTAAATGGAACAACTACTAATCAATGCAGAAATGACGAACTAAATTATCCACCTTAT
TTCCCAGAACTCACAAAAAGAACTGATGGATTACATTTCAGAACAATTTGCATGGAAGCT
GAGCAGATTCTTAGTGATGGAACATCAGTTTTGCATTACGATGTTCACAATCTCTATGGA
TGGTCACAGATGAAACCTACTCATGATGCATTGCAAAAGACAACTGGAAAAAGAGGGATT
GTAATTTCTCGTTCCACGTATCCTACTAGTGGACGATGGGGAGGACACTGGCTTGGAGAC
AACTATGCACGATGGGACAACATGGACAAATCAATCATTGGTATGATGGAATTTAGTCTG
TTTGGAATATCATATACTGGAGCAGACATCTGTGGTTTTTTCAACAACTCAGAATATCAT
CTCTGTACCCGCTGGATGCAACTTGGAGCATTTTATCCATACTCAAGGAATCACAACATT
GCAAATACTAGAAGACAAGATCCCGCTTCCTGGAATGAAACTTTTGCTGAAATGTCAAGG
AATATTCTAAATATTAGATACACCTTATTGCCCTATTTTTACACACAAATGCATGAAATT
CATGCTAATGGTGGCACTGTTATCCGACCCCTTTTGCATGAGTTCTTTGATGAAAAACCA
ACCTGGGATATATTCAAGCAGTTCTTATGGGGTCCAGCATTTATGGTTACCCCAGTACTG
GAACCTTATGTTCAAACTGTAAATGCCTACGTCCCCAATGCTCGGTGGTTTGACTACCAT
ACAGGCAAAGATATTGGCGTCAGAGGACAATTTCAAACATTTAATGCTTCTTATGACACA
ATAAACCTACATGTCCGTGGTGGTCACATCCTACCATGTCAAGAGCCAGCTCAAAACACA
TTTTACAGTCGACAAAAACACATGAAGCTCATTGTTGCTGCAGATGATAATCAGATGGCA
CAGGGTTCTCTGTTTTGGGATGATGGAGAGAGTATAGACACCTATGAAAGAGACCTATAT
TTATCTGTACAATTTAATTTAAACCAGACCACCTTAACAAGCACTATATTGAAGAGAGGT
TACATAAATAAAAGTGAAACGAGGCTTGGATCCCTTCATGTATGGGGGAAAGGAACTACT
CCTGTCAATGCAGTTACTCTAACGTATAACGGAAATAAAAATTCGCTTCCTTTTAATGAA
GACACTACCAACATGATATTACGTATTGATCTGACCACACACAATGTTACTCTAGAAGAA
CCAATAGAAATCAACTGGTCATGA
|
| Enzyme 2 GenBank Gene ID |
X63597  |
| Enzyme 2 GeneCard ID |
SI  |
| Enzyme 2 GenAtlas ID |
SI  |
| Enzyme 2 HGNC ID |
HGNC:10856  |
| Enzyme 2 Chromosome Location |
3 |
| Enzyme 2 Locus |
3q25.2-q26.2 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Chantret I, Lacasa M, Chevalier G, Ruf J, Islam I, Mantei N, Edwards Y, Swallow D, Rousset M: Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem J. 1992 Aug 1;285 ( Pt 3):915-23. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Green F, Edwards Y, Hauri HP, Povey S, Ho MW, Pinto M, Swallow D: Isolation of a cDNA probe for a human jejunal brush-border hydrolase, sucrase-isomaltase, and assignment of the gene locus to chromosome 3. Gene. 1987;57(1):101-10. [PubMed
]
- Gorvel JP, Ferrero A, Chambraud L, Rigal A, Bonicel J, Maroux S: Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon. Gastroenterology. 1991 Sep;101(3):618-25. [PubMed
]
- Ouwendijk J, Moolenaar CE, Peters WJ, Hollenberg CP, Ginsel LA, Fransen JA, Naim HY: Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment. J Clin Invest. 1996 Feb 1;97(3):633-41. [PubMed
]
- Jacob R, Zimmer KP, Schmitz J, Naim HY: Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme. J Clin Invest. 2000 Jul;106(2):281-7. [PubMed
]
- Spodsberg N, Jacob R, Alfalah M, Zimmer KP, Naim HY: Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder. J Biol Chem. 2001 Jun 29;276(26):23506-10. Epub 2001 May 4. [PubMed
]
- Ritz V, Alfalah M, Zimmer KP, Schmitz J, Jacob R, Naim HY: Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum. Gastroenterology. 2003 Dec;125(6):1678-85. [PubMed
]
- Sander P, Alfalah M, Keiser M, Korponay-Szabo I, Kovacs JB, Leeb T, Naim HY: Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption. Hum Mutat. 2006 Jan;27(1):119. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5753 |
| Enzyme 3 Name |
Sorbitol dehydrogenase |
| Enzyme 3 Synonyms |
- L-iditol 2-dehydrogenase
|
| Enzyme 3 Gene Name |
SORD |
| Enzyme 3 Protein Sequence |
>Sorbitol dehydrogenase
MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNF
IVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFC
ATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCG
AGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGQL
GCKPEVTIECTGAEASIQAGIYATRSGGNLVLVGLGSEMTTVPLLHAAIREVDIKGVFRY
CNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP
|
| Enzyme 3 Number of Residues |
357 |
| Enzyme 3 Molecular Weight |
38324.2 |
| Enzyme 3 Theoretical pI |
8.06 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- oxidoreductase activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in zinc ion binding |
| Enzyme 3 Specific Function |
L-iditol + NAD(+) = L-sorbose + NADH |
| Enzyme 3 Pathways |
- Fructose and Mannose Metabolism (map00051
)
|
| Enzyme 3 Reactions |
- L-iditol + NAD+ = L-sorbose + NADH + H+ [RN:R07145]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
156627571  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q00796  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
DHSO_HUMAN  |
| Enzyme 3 PDB ID |
1PL8  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1074 bp
ATGGCGGCGGCGGCCAAGCCCAACAACCTTTCCCTGGTGGTGCACGGACCGGGGGACTTG
CGCCTGGAGAACTATCCTATCCCTGAACCAGGCCCAAATGAGGTCTTGCTGAGGATGCAT
TCTGTTGGAATCTGTGGCTCAGATGTCCACTACTGGGAGTATGGTCGAATTGGGAATTTT
ATTGTGAAAAAGCCCATGGTGCTGGGACATGAAGCTTCGGGAACAGTCGAAAAAGTGGGA
TCATCGGTAAAGCACCTAAAACCAGGTGATCGTGTTGCCATCGAGCCTGGTGCTCCCCGA
GAAAATGATGAATTCTGCAAGATGGGCCGATACAATCTGTCACCTTCCATCTTCTTCTGT
GCCACGCCCCCCGATGACGGGAACCTCTGCCGGTTCTATAAGCACAATGCAGCCTTTTGT
TACAAGCTTCCTGACAATGTCACCTTTGAGGAAGGCGCCCTGATCGAGCCACTTTCTGTG
GGGATCCATGCCTGCAGGAGAGGCGGAGTTACCCTGGGACACAAGGTCCTTGTGTGTGGA
GCTGGGCCAATCGGGATGGTCACTTTGCTCGTGGCCAAAGCAATGGGAGCAGCTCAAGTA
GTGGTGACTGATCTGTCTGCTACCCGATTGTCCAAAGCCAAGGAGATTGGGGCTGATTTA
GTCCTCCAGATCTCCAAGGAGAGCCCTCAGGAAATCGCCAGGAAAGTAGAAGGTCAGCTG
GGGTGCAAGCCGGAAGTCACCATCGAGTGCACGGGGGCAGAGGCCTCCATCCAGGCGGGC
ATCTACGCCACTCGCTCTGGTGGGAACCTCGTGCTTGTGGGGCTGGGCTCTGAGATGACC
ACCGTACCCCTACTGCATGCAGCCATCCGGGAGGTGGATATCAAGGGCGTGTTTCGATAC
TGCAACACGTGGCCAGTGGCGATTTCGATGCTTGCGTCCAAGTCTGTGAATGTAAAACCC
CTCGTCACCCATAGGTTTCCTCTGGAGAAAGCTCTGGAGGCCTTTGAAACATTTAAAAAG
GGATTGGGGTTGAAAATCATGCTCAAGTGTGACCCCAGTGACCAGAATCCCTGA
|
| Enzyme 3 GenBank Gene ID |
NM_003104.5  |
| Enzyme 3 GeneCard ID |
SORD  |
| Enzyme 3 GenAtlas ID |
SORD  |
| Enzyme 3 HGNC ID |
HGNC:11184  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
15q15.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Lee FK, Cheung MC, Chung S: The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization. Genomics. 1994 May 15;21(2):354-8. [PubMed
]
- Iwata T, Popescu NC, Zimonjic DB, Karlsson C, Hoog JO, Vaca G, Rodriguez IR, Carper D: Structural organization of the human sorbitol dehydrogenase gene (SORD). Genomics. 1995 Mar 1;26(1):55-62. [PubMed
]
- Carr IM, Markham AF, Coletta PL: Identification and characterisation of a sequence related to human sorbitol dehydrogenase. Eur J Biochem. 1997 May 1;245(3):760-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Karlsson C, Maret W, Auld DS, Hoog JO, Jornvall H: Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme. Eur J Biochem. 1989 Dec 22;186(3):543-50. [PubMed
]
- 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
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Pauly TA, Ekstrom JL, Beebe DA, Chrunyk B, Cunningham D, Griffor M, Kamath A, Lee SE, Madura R, Mcguire D, Subashi T, Wasilko D, Watts P, Mylari BL, Oates PJ, Adams PD, Rath VL: X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase. Structure. 2003 Sep;11(9):1071-85. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6501 |
| Enzyme 4 Name |
Ketohexokinase |
| Enzyme 4 Synonyms |
- Hepatic fructokinase
|
| Enzyme 4 Gene Name |
KHK |
| Enzyme 4 Protein Sequence |
>Ketohexokinase
MEEKQILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFM
GSMAPGHVADFVLDDLRRYSVDLRYTVFQTTGSVPIATVIINEASGSRTILYYDRSLPDV
SATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPPEQKIRVSVEVEKPREELF
QLFGYGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLL
HSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQGFDGIV
|
| Enzyme 4 Number of Residues |
298 |
| Enzyme 4 Molecular Weight |
32730.1 |
| Enzyme 4 Theoretical pI |
5.72 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Carbohydrate transport and metabolism |
| Enzyme 4 Specific Function |
ATP + D-fructose = ADP + D-fructose 1- phosphate |
| Enzyme 4 Pathways |
- Fructose and Mannose Metabolism (map00051
)
|
| Enzyme 4 Reactions |
- ATP + D-fructose = ADP + D-fructose 1-phosphate [RN:R00866]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
4557693  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P50053  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
KHK_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>897 bp
ATGGAAGAGAAGCAGATCCTGTGCGTGGGGCTAGTGGTGCTGGACGTCATCAGCCTGGTG
GACAAGTACCCTAAGGAGGACTCGGAGATAAGGTGTTTGTCCCAGAGATGGCAGCGCGGA
GGCAACGCGTCCAACTCCTGCACCGTTCTCTCCCTGCTCGGAGCCCCCTGTGCCTTCATG
GGCTCAATGGCTCCTGGCCATGTTGCTGATTTTGTCCTGGATGACCTCCGCCGCTATTCT
GTGGACCTACGCTACACAGTCTTTCAGACCACAGGCTCCGTCCCCATCGCCACGGTCATC
ATCAACGAGGCCAGTGGTAGCCGCACCATCCTATACTATGACAGGAGCCTGCCAGATGTG
TCTGCTACAGACTTTGAGAAGGTTGATCTGACCCAGTTCAAGTGGATCCACATTGAGGGC
CGGAACGCATCGGAGCAGGTGAAGATGCTGCAGCGGATAGACGCACACAACACCAGGCAG
CCTCCAGAGCAGAAGATCCGGGTGTCCGTGGAGGTGGAGAAGCCACGAGAGGAGCTCTTC
CAGCTGTTTGGCTACGGAGACGTGGTGTTTGTCAGCAAAGATGTGGCCAAGCACTTGGGG
TTCCAGTCAGCAGAGGAAGCCTTGAGGGGCTTGTATGGTCGTGTGAGGAAAGGGGCTGTG
CTTGTCTGTGCCTGGGCTGAGGAGGGCGCCGACGCCCTGGGCCCTGATGGCAAATTGCTC
CACTCGGATGCTTTCCCGCCACCCCGCGTGGTGGATACACTGGGAGCTGGAGACACCTTC
AATGCCTCCGTCATCTTCAGCCTCTCCCAGGGGAGGAGCGTGCAGGAAGCACTGAGATTC
GGGTGCCAGGTGGCCGGCAAGAAGTGTGGCCTGCAGGGCTTTGATGGCATCGTGTGA
|
| Enzyme 4 GenBank Gene ID |
NM_000221.2  |
| Enzyme 4 GeneCard ID |
KHK  |
| Enzyme 4 GenAtlas ID |
KHK  |
| Enzyme 4 HGNC ID |
HGNC:6315  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
2p23.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Bonthron DT, Brady N, Donaldson IA, Steinmann B: Molecular basis of essential fructosuria: molecular cloning and mutational analysis of human ketohexokinase (fructokinase). Hum Mol Genet. 1994 Sep;3(9):1627-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hayward BE, Bonthron DT: Structure and alternative splicing of the ketohexokinase gene. Eur J Biochem. 1998 Oct 1;257(1):85-91. [PubMed
]
- Trinh CH, Asipu A, Bonthron DT, Phillips SE: Structures of alternatively spliced isoforms of human ketohexokinase. Acta Crystallogr D Biol Crystallogr. 2009 Mar;65(Pt 3):201-11. Epub 2009 Feb 20. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
12982 |
| Enzyme 5 Name |
Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a) |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
PHPT1 |
| Enzyme 5 Protein Sequence |
>Phosphohistidine phosphatase 1 (Phosphohistidine phosphatase 1, isoform CRA_a)
MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKV
SGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTW
ANDGY
|
| Enzyme 5 Number of Residues |
125 |
| Enzyme 5 Molecular Weight |
13833 |
| Enzyme 5 Theoretical pI |
Not Available |
| Enzyme 5 GO Classification |
Not Available |
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
B1AMX1  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
B1AMX1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
Not Available |
| Enzyme 5 GeneCard ID |
B1AMX1  |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
Not Available |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
13037 |
| Enzyme 6 Name |
Putative uncharacterized protein GAA |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
GAA |
| Enzyme 6 Protein Sequence |
>Putative uncharacterized protein GAA
MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGA
SRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGA
QMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLH
FTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLF
FADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLA
LEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGY
PFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDG
FRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKV
WPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELEN
PPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISR
STFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVR
WTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAG
ETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPV
EALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQP
MALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQ
LQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC
|
| Enzyme 6 Number of Residues |
952 |
| Enzyme 6 Molecular Weight |
105322.9 |
| Enzyme 6 Theoretical pI |
5.91 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in catalytic activity |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
119393891  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
A6NFM4  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
A6NFM4_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2859 bp
ATGGGAGTGAGGCACCCGCCCTGCTCCCACCGGCTCCTGGCCGTCTGCGCCCTCGTGTCC
TTGGCAACCGCTGCACTCCTGGGGCACATCCTACTCCATGATTTCCTGCTGGTTCCCCGA
GAGCTGAGTGGCTCCTCCCCAGTCCTGGAGGAGACTCACCCAGCTCACCAGCAGGGAGCC
AGCAGACCAGGGCCCCGGGATGCCCAGGCACACCCCGGCCGTCCCAGAGCAGTGCCCACA
CAGTGCGACGTCCCCCCCAACAGCCGCTTCGATTGCGCCCCTGACAAGGCCATCACCCAG
GAACAGTGCGAGGCCCGCGGCTGTTGCTACATCCCTGCAAAGCAGGGGCTGCAGGGAGCC
CAGATGGGGCAGCCCTGGTGCTTCTTCCCACCCAGCTACCCCAGCTACAAGCTGGAGAAC
CTGAGCTCCTCTGAAATGGGCTACACGGCCACCCTGACCCGTACCACCCCCACCTTCTTC
CCCAAGGACATCCTGACCCTGCGGCTGGACGTGATGATGGAGACTGAGAACCGCCTCCAC
TTCACGATCAAAGATCCAGCTAACAGGCGCTACGAGGTGCCCTTGGAGACCCCGCATGTC
CACAGCCGGGCACCGTCCCCACTCTACAGCGTGGAGTTCTCCGAGGAGCCCTTCGGGGTG
ATCGTGCGCCGGCAGCTGGACGGCCGCGTGCTGCTGAACACGACGGTGGCGCCCCTGTTC
TTTGCGGACCAGTTCCTTCAGCTGTCCACCTCGCTGCCCTCGCAGTATATCACAGGCCTC
GCCGAGCACCTCAGTCCCCTGATGCTCAGCACCAGCTGGACCAGGATCACCCTGTGGAAC
CGGGACCTTGCGCCCACGCCCGGTGCGAACCTCTACGGGTCTCACCCTTTCTACCTGGCG
CTGGAGGACGGCGGGTCGGCACACGGGGTGTTCCTGCTAAACAGCAATGCCATGGATGTG
GTCCTGCAGCCGAGCCCTGCCCTTAGCTGGAGGTCGACAGGTGGGATCCTGGATGTCTAC
ATCTTCCTGGGCCCAGAGCCCAAGAGCGTGGTGCAGCAGTACCTGGACGTTGTGGGATAC
CCGTTCATGCCGCCATACTGGGGCCTGGGCTTCCACCTGTGCCGCTGGGGCTACTCCTCC
ACCGCTATCACCCGCCAGGTGGTGGAGAACATGACCAGGGCCCACTTCCCCCTGGACGTC
CAGTGGAACGACCTGGACTACATGGACTCCCGGAGGGACTTCACGTTCAACAAGGATGGC
TTCCGGGACTTCCCGGCCATGGTGCAGGAGCTGCACCAGGGCGGCCGGCGCTACATGATG
ATCGTGGATCCTGCCATCAGCAGCTCGGGCCCTGCCGGGAGCTACAGGCCCTACGACGAG
GGTCTGCGGAGGGGGGTTTTCATCACCAACGAGACCGGCCAGCCGCTGATTGGGAAGGTA
TGGCCCGGGTCCACTGCCTTCCCCGACTTCACCAACCCCACAGCCCTGGCCTGGTGGGAG
GACATGGTGGCTGAGTTCCATGACCAGGTGCCCTTCGACGGCATGTGGATTGACATGAAC
GAGCCTTCCAACTTCATCAGGGGCTCTGAGGACGGCTGCCCCAACAATGAGCTGGAGAAC
CCACCCTACGTGCCTGGGGTGGTTGGGGGGACCCTCCAGGCGGCCACCATCTGTGCCTCC
AGCCACCAGTTTCTCTCCACACACTACAACCTGCACAACCTCTACGGCCTGACCGAAGCC
ATCGCCTCCCACAGGGCGCTGGTGAAGGCTCGGGGGACACGCCCATTTGTGATCTCCCGC
TCGACCTTTGCTGGCCACGGCCGATACGCCGGCCACTGGACGGGGGACGTGTGGAGCTCC
TGGGAGCAGCTCGCCTCCTCCGTGCCAGAAATCCTGCAGTTTAACCTGCTGGGGGTGCCT
CTGGTCGGGGCCGACGTCTGCGGCTTCCTGGGCAACACCTCAGAGGAGCTGTGTGTGCGC
TGGACCCAGCTGGGGGCCTTCTACCCCTTCATGCGGAACCACAACAGCCTGCTCAGTCTG
CCCCAGGAGCCGTACAGCTTCAGCGAGCCGGCCCAGCAGGCCATGAGGAAGGCCCTCACC
CTGCGCTACGCACTCCTCCCCCACCTCTACACACTGTTCCACCAGGCCCACGTCGCGGGG
GAGACCGTGGCCCGGCCCCTCTTCCTGGAGTTCCCCAAGGACTCTAGCACCTGGACTGTG
GACCACCAGCTCCTGTGGGGGGAGGCCCTGCTCATCACCCCAGTGCTCCAGGCCGGGAAG
GCCGAAGTGACTGGCTACTTCCCCTTGGGCACATGGTACGACCTGCAGACGGTGCCAGTA
GAGGCCCTTGGCAGCCTCCCACCCCCACCTGCAGCTCCCCGTGAGCCAGCCATCCACAGC
GAGGGGCAGTGGGTGACGCTGCCGGCCCCCCTGGACACCATCAACGTCCACCTCCGGGCT
GGGTACATCATCCCCCTGCAGGGCCCTGGCCTCACAACCACAGAGTCCCGCCAGCAGCCC
ATGGCCCTGGCTGTGGCCCTGACCAAGGGTGGGGAGGCCCGAGGGGAGCTGTTCTGGGAC
GATGGAGAGAGCCTGGAAGTGCTGGAGCGAGGGGCCTACACACAGGTCATCTTCCTGGCC
AGGAATAACACGATCGTGAATGAGCTGGTACGTGTGACCAGTGAGGGAGCTGGCCTGCAG
CTGCAGAAGGTGACTGTCCTGGGCGTGGCCACGGCGCCCCAGCAGGTCCTCTCCAACGGT
GTCCCTGTCTCCAACTTCACCTACAGCCCCGACACCAAGGTCCTGGACATCTGTGTCTCG
CTGTTGATGGGAGAGCAGTTTCTCGTCAGCTGGTGTTAG
|
| Enzyme 6 GenBank Gene ID |
NM_000152.3  |
| Enzyme 6 GeneCard ID |
GAA  |
| Enzyme 6 GenAtlas ID |
GAA  |
| Enzyme 6 HGNC ID |
HGNC:4065  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
17q25.2-q25.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
21022 |
| Enzyme 7 Name |
14 kDa phosphohistidine phosphatase |
| Enzyme 7 Synonyms |
- Phosphohistidine phosphatase 1
- Protein janus-A homolog
|
| Enzyme 7 Gene Name |
PHPT1 |
| Enzyme 7 Protein Sequence |
>14 kDa phosphohistidine phosphatase
MAVADLALIPDVDIDSDGVFKYVLIRVHSAPRSGAPAAESKEIVRGYKWAEYHADIYDKV
SGDMQKQGCDCECLGGGRISHQSQDKKIHVYGYSMAYGPAQHAISTEKIKAKYPDYEVTW
ANDGY
|
| Enzyme 7 Number of Residues |
125 |
| Enzyme 7 Molecular Weight |
13832.4 |
| Enzyme 7 Theoretical pI |
5.98 |
| Enzyme 7 GO Classification |
Not Available |
| Enzyme 7 General Function |
Involved in phosphohistidine phosphatase activity |
| Enzyme 7 Specific Function |
Exhibits phosphohistidine phosphatase activity |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
8895093  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9NRX4  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PHP14_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>378 bp
ATGGCGGTGGCGGACCTCGCTCTCATTCCTGATGTGGACATCGACTCCGACGGCGTCTTC
AAGTATGTGCTGATCCGAGTCCACTCGGCTCCCCGCTCCGGGGCTCCGGCTGCAGAGAGC
AAGGAGATCGTGCGCGGCTACAAGTGGGCTGAGTACCATGCGGACATCTACGACAAAGTG
TCGGGCGACATGCAGAAGCAAGGCTGCGACTGTGAGTGTCTGGGCGGCGGGCGCATCTCC
CACCAGAGTCAGGACAAGAAGATTCACGTGTACGGCTATTCCATGGCCTATGGTCCTGCC
CAGCACGCCATTTCAACTGAGAAAATCAAAGCCAAGTACCCCGACTACGAGGTCACCTGG
GCTAACGACGGCTACTGA
|
| Enzyme 7 GenBank Gene ID |
AF164795  |
| Enzyme 7 GeneCard ID |
PHPT1  |
| Enzyme 7 GenAtlas ID |
PHPT1  |
| Enzyme 7 HGNC ID |
HGNC:30033  |
| Enzyme 7 Chromosome Location |
9 |
| Enzyme 7 Locus |
9q34.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Ek P, Pettersson G, Ek B, Gong F, Li JP, Zetterqvist O: Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase. Eur J Biochem. 2002 Oct;269(20):5016-23. [PubMed
]
- 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
]
- Lai CH, Chiu JY, Lin W: Identification of the human crooked neck gene by comparative gene identification. Biochim Biophys Acta. 2001 Feb 16;1517(3):449-54. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ma R, Kanders E, Sundh UB, Geng M, Ek P, Zetterqvist O, Li JP: Mutational study of human phosphohistidine phosphatase: effect on enzymatic activity. Biochem Biophys Res Commun. 2005 Nov 25;337(3):887-91. Epub 2005 Sep 30. [PubMed
]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed
]
- Busam RD, Thorsell AG, Flores A, Hammarstrom M, Persson C, Hallberg BM: First structure of a eukaryotic phosphohistidine phosphatase. J Biol Chem. 2006 Nov 10;281(45):33830-4. Epub 2006 Sep 21. [PubMed
]
- Gong W, Li Y, Cui G, Hu J, Fang H, Jin C, Xia B: Solution structure and catalytic mechanism of human protein histidine phosphatase 1. Biochem J. 2009 Mar 1;418(2):337-44. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |