|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5392 |
| Enzyme 1 Name |
Methionine synthase |
| Enzyme 1 Synonyms |
- 5-methyltetrahydrofolate--homocysteine methyltransferase
- Vitamin-B12 dependent methionine synthase
- MS
|
| Enzyme 1 Gene Name |
MTR |
| Enzyme 1 Protein Sequence |
>Methionine synthase
MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHA
RPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMC
SAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQA
KGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQT
GEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDET
PSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGL
EPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDG
MLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDD
FLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNI
LTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLY
HAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKV
IQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVG
DLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATV
KGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEM
IFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDEN
LKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQV
FEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTL
ISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYY
CLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE
LHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTG
IRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPIL
GYDTD
|
| Enzyme 1 Number of Residues |
1265 |
| Enzyme 1 Molecular Weight |
140525.9 |
| Enzyme 1 Theoretical pI |
5.27 |
| Enzyme 1 GO Classification |
| Function |
- S-methyltransferase activity
- binding
- catalytic activity
- cation binding
- cobalamin binding
- homocysteine S-methyltransferase activity
- ion binding
- metal ion binding
- methionine synthase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- vitamin binding
- zinc ion binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- metabolic process
- methionine biosynthetic process
- pteridine and derivative metabolic process
- sulfur amino acid biosynthetic process
- sulfur amino acid metabolic process
|
| Component |
|
|
| Enzyme 1 General Function |
Involved in cobalamin binding |
| Enzyme 1 Specific Function |
Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine [RN:R00946]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q99707  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
METH_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>3798 bp
ATGTCACCCGCGCTCCAAGACCTGTCGCAACCCGAAGGTCTGAAGAAAACCCTGCGGGAT
GAGATCAATGCCATTCTGCAGAAGAGGATTATGGTGCTGGATGGAGGGATGGGGACCATG
ATCCAGCGGGAGAAGCTAAACGAAGAACACTTCCGAGGTCAGGAATTTAAAGATCATGCC
AGGCCGCTGAAAGGCAACAATGACATTTTAAGTATAACTCAGCCTGATGTCATTTACCAA
ATCCATAAGGAATACTTGCTGGCTGGGGCAGATATCATTGAAACAAATACTTTTAGCAGC
ACTAGTATTGCCCAAGCTGACTATGGCCTTGAACACTTGGCCTACCGGATGAACATGTGC
TCTGCAGGAGTGGCCAGAAAAGCTGCCGAGGAGGTAACTCTCCAGACAGGAATTAAGAGG
TTTGTGGCAGGGGCTCTGGGTCCGACTAATAAGACACTCTCTGTGTCCCCATCTGTGGAA
AGGCCGGATTATAGGAACATCACATTTGATGAGCTTGTTGAAGCATACCAAGAGCAGGCC
AAAGGACTTCTGGATGGCGGGGTTGATATCTTACTCATTGAAACTATTTTTGATACTGCC
AATGCCAAGGCAGCCTTGTTTGCACTCCAAAATCTTTTTGAGGAGAAATATGCTCCCCGG
CCTATCTTTATTTCAGGGACGATCGTTGATAAAAGTGGGCGGACTCTTTCCGGACAGACA
GGAGAGGGATTTGTCATCAGCGTGTCTCATGGAGAACCACTCTGCATTGGATTAAATTGT
GCTTTGGGTGCAGCTGAGATGAGACCTTTTATTGAAATAATTGGAAAATGTACAACAGCC
TATGTCCTCTGTTATCCCAATGCAGGTCTTCCCAACACCTTTGGTGACTATGATGAAACG
CCTTCTATGATGGCCAAGCACCTAAAGGATTTTGCTATGGATGGCTTGGTCAATATAGTT
GGAGGATGCTGTGGGTCAACACCAGATCATATCAGGGAAATTGCTGAAGCTGTGAAAAAT
TGTAAGCCTAGAGTTCCACCTGCCACTGCTTTTGAAGGACATATGTTACTGTCTGGTCTA
GAGCCCTTCAGGATTGGACCGTACACCAACTTTGTTAACATTGGAGAGCGCTGTAATGTT
GCAGGATCAAGGAAGTTTGCTAAACTCATCATGGCAGGAAACTATGAAGAAGCCTTGTGT
GTTGCCAAAGTGCAGGTGGAAATGGGAGCCCAGGTGTTGGATGTCAACATGGATGATGGC
ATGCTAGATGGTCCAAGTGCAATGACCAGATTTTGCAACTTAATTGCTTCCGAGCCAGAC
ATCGCAAAGGTACCTTTGTGCATCGACTCCTCCAATTTTGCTGTGATTGAAGCTGGGTTA
AAGTGCTGCCAAGGGAAGTGCATTGTCAATAGCATTAGTCTGAAGGAAGGAGAGGACGAC
TTCTTGGAGAAGGCCAGGAAGATTAAAAAGTATGGAGCTGCTATGGTGGTCATGGCTTTT
GATGAAGAAGGACAGGCAACAGAAACAGACACAAAAATCAGAGTGTGCACCCGGGCCTAC
CATCTGCTTGTGAAAAAACTGGGCTTTAATCCAAATGACATTATTTTTGACCCTAATATC
CTAACCATTGGGACTGGAATGGAGGAACACAACTTGTATGCCATTAATTTTATCCATGCA
ACAAAAGTCATTAAAGAAACATTACCTGGAGCCAGAATAAGTGGAGGTCTTTCCAACTTG
TCCTTCTCCTTCCGAGGAATGGAAGCCATTCGAGAAGCAATGCATGGGGTTTTCCTTTAC
CATGCAATCAAGTCTGGCATGGACATGGGGATAGTGAATGCTGGAAACCTCCCTGTGTAT
GATGATATCCATAAGGAACTTCTGCAGCTCTGTGAAGATCTCATCTGGAATAAAGACCCT
GAGGCCACTGAGAAGCTCTTACGTTATGCCCAGACTCAAGGCACAGGAGGGAAGAAAGTC
ATTCAGACTGATGAGTGGAGAAATGGCCCTGTCGAAGAACGCCTTGAGTATGCCCTTGTG
AAGGGCATTGAAAAACATATTATTGAGGATACTGAGGAAGCCAGGTTAAACCAAAAAAAA
TATCCCCGACCTCTCAATATAATTGAAGGACCCCTGATGAATGGAATGAAAATTGTTGGT
GATCTTTTTGGAGCTGGAAAAATGTTTCTACCTCAGGTTATAAAGTCAGCCCGGGTTATG
AAGAAGGCTGTTGGCCACCTTATCCCTTTCATGGAAAAAGAAAGAGAAGAAACCAGAGTG
CTTAACGGCACAGTAGAAGAAGAGGACCCTTACCAGGGCACCATCGTGCTGGCCACTGTT
AAAGGCGACGTGCACGACATAGGCAAGAACATAGTTGGAGTAGTCCTTGGCTGCAATAAT
TTCCGAGTTATTGATTTAGGAGTCATGACTCCATGTGATAAGATACTGAAAGCTGCTCTT
GACCACAAAGCAGATATAATTGGCCTGTCAGGACTCATCACTCCTTCCCTGGATGAAATG
ATTTTTGTTGCCAAGGAAATGGAGAGATTAGCTATAAGGATTCCATTGTTGATTGGAGGA
GCAACCACTTCAAAAACCCACACAGCAGTTAAAATAGCTCCGAGATACAGTGCACCTGTA
ATCCATGTCCTGGACGCGTCCAAGAGTGTGGTGGTGTGTTCCCAGCTGTTAGATGAAAAT
CTAAAGGATGAATACTTTGAGGAAATCATGGAAGAATATGAAGATATTAGACAGGACCAT
TATGAGTCTCTCAAGGAGAGGAGATACTTACCCTTAAGTCAAGCCAGAAAAAGTGGTTTC
CAAATGGATTGGCTGTCTGAACCTCACCCAGTGAAGCCCACGTTTATTGGGACCCAGGTC
TTTGAAGACTATGACCTGCAGAAGCTGGTGGACTACATTGACTGGAAGCCTTTCTTTGAT
GTCTGGCAGCTCCGGGGCAAGTACCCGAATCGAGGCTTCCCCAAGATATTTAACGACAAA
ACAGTAGGTGGAGAGGCCAGGAAGGTCTACGATGATGCCCACAATATGCTGAACACACTG
ATTAGTCAAAAGAAACTCCGGGCCCGGGGTGTGGTTGGGTTCTGGCCAGCACAGAGTATC
CAAGACGACATTCACCTGTACGCAGAGGCTGCTGTGCCCCAGGCTGCAGAGCCCATAGCC
ACTTTCTATGGGTTAAGGCAACAGGCTGAGAAGGACTCTGCCAGCACGGAGCCATACTAC
TGCCTCTCAGACTTCATCGCTCCCTTGCATTCTGGCATCCGTGACTACCTGGGCCTGTTT
GCCGTTGCCTGCTTTGGGGTAGAAGAGCTGAGCAAGGCCTATGAGGATGATGGTGACGAC
TACAGCAGCATCATGGTCAAGGCGCTGGGGGACCGGCTGGCAGAGGCCTTTGCAGAAGAG
CTCCATGAAAGAGTTCGCCGAGAACTGTGGGCCTACTGTGGCAGTGAGCAGCTGGACGTC
GCAGACCTGCGAAGGTTGCGGTACAAGGGCATCCGCCCGGCTCCTGGCTACCCCAGCCAG
CCCGACCACACCGAGAAGCTCACCATGTGGAGACTCGCAGACATCGAGCAGTCTACAGGC
ATTAGGTTAACAGAATCATTAGCAATGGCACCTGCTTCAGCAGTCTCAGGCCTCTACTTC
TCCAATTTGAAGTCCAAATATTTTGCTGTGGGGAAGATTTCCAAGGATCAGGTTGAGGAT
TATGCATTGAGGAAGAACATATCTGTGGCTGAGGTTGAGAAATGGCTTGGACCCATTTTG
GGATATGATACAGACTAA
|
| Enzyme 1 GenBank Gene ID |
U71285  |
| Enzyme 1 GeneCard ID |
MTR  |
| Enzyme 1 GenAtlas ID |
MTR  |
| Enzyme 1 HGNC ID |
HGNC:7468  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1q43 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Leclerc D, Campeau E, Goyette P, Adjalla CE, Christensen B, Ross M, Eydoux P, Rosenblatt DS, Rozen R, Gravel RA: Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. Hum Mol Genet. 1996 Dec;5(12):1867-74. [PubMed
]
- Li YN, Gulati S, Baker PJ, Brody LC, Banerjee R, Kruger WD: Cloning, mapping and RNA analysis of the human methionine synthase gene. Hum Mol Genet. 1996 Dec;5(12):1851-8. [PubMed
]
- Chen LH, Liu ML, Hwang HY, Chen LS, Korenberg J, Shane B: Human methionine synthase. cDNA cloning, gene localization, and expression. J Biol Chem. 1997 Feb 7;272(6):3628-34. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [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
]
- Gulati S, Baker P, Li YN, Fowler B, Kruger W, Brody LC, Banerjee R: Defects in human methionine synthase in cblG patients. Hum Mol Genet. 1996 Dec;5(12):1859-65. [PubMed
]
- Doolin MT, Barbaux S, McDonnell M, Hoess K, Whitehead AS, Mitchell LE: Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. Am J Hum Genet. 2002 Nov;71(5):1222-6. Epub 2002 Oct 9. [PubMed
]
- O'Leary VB, Mills JL, Pangilinan F, Kirke PN, Cox C, Conley M, Weiler A, Peng K, Shane B, Scott JM, Parle-McDermott A, Molloy AM, Brody LC: Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association. Mol Genet Metab. 2005 Jul;85(3):220-7. Epub 2005 Mar 17. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5509 |
| Enzyme 2 Name |
Tyrosine aminotransferase |
| Enzyme 2 Synonyms |
- TAT
- L-tyrosine:2-oxoglutarate aminotransferase
|
| Enzyme 2 Gene Name |
TAT |
| Enzyme 2 Protein Sequence |
>Tyrosine aminotransferase
MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
|
| Enzyme 2 Number of Residues |
454 |
| Enzyme 2 Molecular Weight |
50398.9 |
| Enzyme 2 Theoretical pI |
6.24 |
| Enzyme 2 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- L-tyrosine aminotransferase activity
- L-tyrosine:2-oxoglutarate aminotransferase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- aromatic amino acid family catabolic process
- aromatic amino acid family metabolic process
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid catabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in 1-aminocyclopropane-1-carboxylate synthase activity |
| Enzyme 2 Specific Function |
Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has no transaminase activity towards phenylalanine |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate [RN:R00734]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
36713  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P17735  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ATTY_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1365 bp
ATGGACCCATACATGATTCAGATGAGCAGCAAAGGCAACCTCCCCTCAATTCTGGACGTG
CATGTCAACGTTGGTGGGAGAAGCTCTGTGCCGGGAAAAATGAAAGGCAGAAAGGCCAGG
TGGTCTGTGAGGCCCTCAGACATGGCCAAGAAAACTTTCAACCCCATCCGAGCCATTGTG
GACAACATGAAGGTGAAACCAAATCCAAACAAAACCATGATTTCCCTGTCCATTGGGGAC
CCTACTGTGTTTGGAAACCTGCCTACAGACCCTGAAGTTACCCAGGCAATGAAAGATGCC
CTGGACTCGGGCAAATATAATGGCTATGCCCCATCCATCGGCTTCCTATCCAGTCGGGAG
GAGATTGCTTCTTATTACCACTGTCCTGAGGCACCCCTAGAAGCTAAGGACGTCATTCTG
ACAAGTGGCTGCAGCCAAGCTATTGACCTTTGTTTAGCTGTGTTGGCCAACCCAGGGCAG
AACATCCTGGTTCCAAGACCTGGTTTCTCTCTCTACAAGACTCTGGCTGAGTCTATGGGA
ATTGAGGTCAAACTCTACAATTTGTTGCCAGAGAAATCTTGGGAAATTGACCTGAAACAA
CTGGAATATCTAATTGATGAAAAGACAGCTTGTCTCATTGTCAATAATCCATCAAACCCC
TGTGGGTCAGTGTTCAGCAAACGTCATCTTCAGAAGATTCTGGCAGTGGCTGCACGGCAG
TGTGTCCCCATCTTAGCTGATGAGATCTATGGAGACATGGTGTTTTCGGATTGCAAATAT
GAACCACTGGCCACCCTCAGCACCGATGTCCCCATCCTGTCCTGTGGAGGGCTGGCCAAG
CGCTGGCTGGTTCCTGGCTGGAGGTTGGGCTGGATCCTCATTCATGACCGAAGAGACATT
TTTGGCAATGAGATCCGAGATGGGCTGGTGAAGCTGAGTCAGCGCATTTTGGGACCCTGT
ACCATTGTCCAGGGAGCTCTGAAAAGCATCCTATGTCGCACCCCGGGAGAGTTTTACCAC
AACACTCTGAGCTTCCTCAAGTCCAATGCTGATCTCTGTTATGGGGCGTTGGCTGCCATC
CCTGGACTCCGGCCAGTCCGCCCTTCTGGGGCTATGTACCTCATGGTTGGAATTGAGATG
GAACATTTCCCAGAATTTGAGAACGATGTGGAGTTCACGGAGCGGTTAGTTGCTGAGCAG
TCTGTCCACTGCCTCCCAGCAACGTGCTTTGAGTACCCGAATTTCATCCGAGTGGTCATC
ACAGTCCCCGAGGTGATGATGCTGGAGGCGTGCAGCCGGATCCAGGAGTTCTGTGAGCAG
CACTACCATTGTGCTGAAGGCAGCCAGGAGGAGTGTGATAAATAG
|
| Enzyme 2 GenBank Gene ID |
X52520  |
| Enzyme 2 GeneCard ID |
TAT  |
| Enzyme 2 GenAtlas ID |
TAT  |
| Enzyme 2 HGNC ID |
HGNC:11573  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
16q22.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Rettenmeier R, Natt E, Zentgraf H, Scherer G: Isolation and characterization of the human tyrosine aminotransferase gene. Nucleic Acids Res. 1990 Jul 11;18(13):3853-61. [PubMed
]
- Zelenin SM, Mertvetsov NP: [Nucleotide sequence of the human tyrosine aminotransferase gene] Bioorg Khim. 1994 Feb;20(2):196-204. [PubMed
]
- Seralini GE, Luu-The V, Labrie F: Cloning and expression of human tyrosine aminotransferase cDNA. Biochim Biophys Acta. 1995 Jan 2;1260(1):97-101. [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
]
- Sivaraman S, Kirsch JF: The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II. FEBS J. 2006 May;273(9):1920-9. [PubMed
]
- Natt E, Kida K, Odievre M, Di Rocco M, Scherer G: Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9297-301. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5642 |
| Enzyme 3 Name |
S-adenosylmethionine synthase isoform type-2 |
| Enzyme 3 Synonyms |
- AdoMet synthase 2
- Methionine adenosyltransferase 2
- MAT 2
- Methionine adenosyltransferase II
- MAT-II
|
| Enzyme 3 Gene Name |
MAT2A |
| Enzyme 3 Protein Sequence |
>S-adenosylmethionine synthase isoform type-2
MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVA
KTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQG
VHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDS
KTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDT
IYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVI
VRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
|
| Enzyme 3 Number of Residues |
395 |
| Enzyme 3 Molecular Weight |
43660.4 |
| Enzyme 3 Theoretical pI |
6.45 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- methionine adenosyltransferase activity
- nucleoside binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- cellular metabolic process
- metabolic process
- one-carbon metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in methionine adenosyltransferase activity |
| Enzyme 3 Specific Function |
Catalyzes the formation of S-adenosylmethionine from methionine and ATP |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine [RN:R00177]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
36327  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P31153  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
METK2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1188 bp
ATGAACGGACAGCTCAACGGCTTCCACGAGGCGTTCATCGAGGAGGGCACATTCCTTTTC
ACCTCAGAGTCGGTCGGGGAAGGCCACCCAGATAAGATTTGTGACCAAATCAGTGATGCT
GTCCTTGATGCCCACCTTCAGCAGGATCCTGATGCCAAAGTAGCTTGTGAAACTGTTGCT
AAAACTGGAATGATCCTTCTTGCTGGGGAAATTACATCCAGAGCTGCTGTTGACTACCAG
AAAGTGGTTCGTGAAGCTGTTAAACACATTGGATATGATGATTCTTCCAAAGGTTTTGAC
TACAAGACTTGTAACGTGCTGGTAGCCTTGGAGCAACAGTCACCAGATATTGCTCAAGGT
GTTCATCTTGACAGAAATGAAGAAGACATTGGTGCTGGAGACCAGGGCTTAATGTTTGGC
TATGCCACTGATGAAACTGAGGAGTGTATGCCTTTAACCATTGTCTTGGCACACAAGCTA
AATGCCAAACTGGCAGAACTACGCCGTAATGGCACTTTGCCTTGGTTACGCCCTGATTCT
AAAACTCAAGTTACTGTGCAGTATATGCAGGATCGAGGTGCTGTGCTTCCCATCAGAGTC
CACACAATTGTTATATCTGTTCAGCATGATGAAGAGGTTTGTCTTGATGAAATGAGGGAT
GCCCTAAAGGAGAAAGTCATCAAAGCAGTTGTGCCTGCGAAATACCTTGATGAGGATACA
ATCTACCACCTACAGCCAAGTGGCAGATTTGTTATTGGTGGGCCTCAGGGTGATGCTGGT
TTGACTGGACGGAAAATCATTGTGGACACTTATGGCGGTTGGGGTGCTCATGGAGGAGGT
GCCTTTTCAGGAAAGGATTATACCAAGGTCGACCGTTCAGCTGCTTATGCTGCTCGTTGG
GTGGCAAAATCCCTTGTTAAAGGAGGTCTGTGCCGGAGGGTTCTTGTTCAGGTCTCTTAT
GCTATTGGAGTTTCTCATCCATTATCTATCTCCATTTTCCATTATGGTACCTCTCAGAAG
AGTGAGAGAGAGCTATTAGAGATTGTGAAGAAGAATTTCGATCTCCGCCCTGGGGTCATT
GTCAGGGATCTGGATCTGAAGAAGCCAATTTATCAGAGGACTGCAGCCTATGGCCACTTT
GGTAGGGACAGCTTCCCATGGGAAGTGCCCAAAAAGCTTAAATATTGA
|
| Enzyme 3 GenBank Gene ID |
X68836  |
| Enzyme 3 GeneCard ID |
MAT2A  |
| Enzyme 3 GenAtlas ID |
MAT2A  |
| Enzyme 3 HGNC ID |
HGNC:6904  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
2p11.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Horikawa S, Tsukada K: Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase. FEBS Lett. 1992 Nov 2;312(1):37-41. [PubMed
]
- Panayiotidis MI, Stabler SP, Ahmad A, Pappa A, Legros LH Jr, Hernandez-Saavedra D, Schneider BK, Allen RH, Vasiliou V, McCord JM, Kotb M, White CW: Activation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia. Free Radic Biol Med. 2006 Jan 15;40(2):348-58. Epub 2005 Nov 18. [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
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [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
]
- LeGros HL Jr, Halim AB, Geller AM, Kotb M: Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II). J Biol Chem. 2000 Jan 28;275(4):2359-66. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5645 |
| Enzyme 4 Name |
Arsenite methyltransferase |
| Enzyme 4 Synonyms |
- Methylarsonite methyltransferase
- S-adenosyl-L-methionine:arsenic(III) methyltransferase
|
| Enzyme 4 Gene Name |
AS3MT |
| Enzyme 4 Protein Sequence |
>Arsenite methyltransferase
MAALRDAEIQKDVQTYYGQVLKRSADLQTNGCVTTARPVPKHIREALQNVHEEVALRYYG
CGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHME
KYGFQASNVTFIHGYIEKLGEAGIKNESHDIVVSNCVINLVPDKQQVLQEAYRVLKHGGE
LYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFCPPRLVTANLITIQN
KELERVIGDCRFVSATFRLFKHSKTGPTKRCQVIYNGGITGHEKELMFDANFTFKEGEIV
EVDEETAAILKNSRFAQDFLIRPIGEKLPTSGGCSALELKDIITDPFKLAEESDSMKSRC
VPDAAGGCCGTKKSC
|
| Enzyme 4 Number of Residues |
375 |
| Enzyme 4 Molecular Weight |
41747.5 |
| Enzyme 4 Theoretical pI |
6.14 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in methyltransferase activity |
| Enzyme 4 Specific Function |
Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me- AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
- (1) S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate [RN:R05755]
- (2) S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate [RN:R05756]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
109389364  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9HBK9  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
AS3MT_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1128 bp
ATGGCTGCACTTCGTGACGCTGAGATACAGAAGGACGTGCAGACCTACTACGGGCAGGTG
CTGAAGAGATCGGCAGACCTCCAGACCAACGGCTGTGTCACCACAGCCAGGCCGGTCCCC
AAGCACATCCGGGAAGCCTTGCAAAATGTACACGAAGAAGTAGCCCTAAGATATTATGGC
TGTGGTCTGGTGATCCCTGAGCATCTAGAAAACTGCTGGATTTTGGATCTGGGTAGTGGA
AGTGGCAGAGATTGCTATGTACTTAGCCAGCTGGTTGGTGAAAAAGGACACGTGACTGGA
ATAGACATGACCAAAGGCCAGGTGGAAGTGGCTGAAAAGTATCTTGACTATCACATGGAA
AAATATGGCTTCCAGGCATCTAATGTGACTTTTATTCATGGCTACATTGAGAAGTTGGGA
GAGGCTGGAATCAAGAATGAGAGCCATGATATTGTTGTATCAAACTGTGTTATTAACCTT
GTGCCTGATAAACAACAAGTGCTTCAGGAGGCATATCGGGTGCTGAAGCATGGTGGGGAG
TTATATTTCAGTGACGTCTATACGAGCCTTGAACTGCCAGAAGAAATCAGGACACACAAA
GTTTTATGGGGTGAGTGTCTGGGTGGTGCTTTATACTGGAAGGAACTTGCTGTCCTTGCT
CAAAAAATTGGGTTCTGCCCTCCACGTTTGGTCACTGCCAATCTCATTACAATTCAAAAC
AAGGAACTGGAAAGAGTTATCGGTGACTGTCGTTTTGTTTCTGCAACATTTCGCCTCTTC
AAACACTCTAAGACAGGACCAACCAAGAGATGCCAAGTTATTTACAATGGAGGAATTACA
GGACATGAAAAAGAACTAATGTTTGATGCCAATTTTACATTTAAGGAAGGTGAAATTGTT
GAAGTGGATGAAGAAACAGCAGCTATCTTGAAGAATTCAAGATTTGCTCAAGATTTTCTG
ATCAGACCAATTGGAGAGAAGTTGCCAACATCTGGAGGCTGTTCTGCTTTGGAGTTAAAG
GATATAATCACAGATCCATTTAAGCTTGCAGAAGAGTCTGACAGTATGAAGTCCAGATGT
GTCCCTGATGCTGCTGGAGGCTGCTGTGGCACAAAGAAAAGCTGCTAA
|
| Enzyme 4 GenBank Gene ID |
NM_020682.3  |
| Enzyme 4 GeneCard ID |
AS3MT  |
| Enzyme 4 GenAtlas ID |
AS3MT  |
| Enzyme 4 HGNC ID |
HGNC:17452  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
10q24.32 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Wood TC, Salavagionne OE, Mukherjee B, Wang L, Klumpp AF, Thomae BA, Eckloff BW, Schaid DJ, Wieben ED, Weinshilboum RM: Human arsenic methyltransferase (AS3MT) pharmacogenetics: gene resequencing and functional genomics studies. J Biol Chem. 2006 Mar 17;281(11):7364-73. Epub 2006 Jan 6. [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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5652 |
| Enzyme 5 Name |
Indolethylamine N-methyltransferase |
| Enzyme 5 Synonyms |
- Indolamine N-methyltransferase
- Aromatic alkylamine N-methyltransferase
- Amine N-methyltransferase
- Arylamine N-methyltransferase
|
| Enzyme 5 Gene Name |
INMT |
| Enzyme 5 Protein Sequence |
>Indolethylamine N-methyltransferase
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLI
DIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGN
SGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAAL
CNLASLLKPGGHLVTTVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQ
SYSVTNAANNGVCFIVARKKPGP
|
| Enzyme 5 Number of Residues |
263 |
| Enzyme 5 Molecular Weight |
28890.8 |
| Enzyme 5 Theoretical pI |
4.92 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in methyltransferase activity |
| Enzyme 5 Specific Function |
Catalyzes the N-methylation of tryptamine and structurally related compounds (Potential) |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + a methylated amine [RN:R02808]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
66933018  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
O95050  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
INMT_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>792 bp
ATGAAGGGTGGCTTCACTGGGGGTGATGAGTACCAGAAGCACTTCCTGCCCAGGGACTAC
TTGGCTACTTACTACAGCTTCGATGGCAGCCCCTCACCCGAGGCCGAGATGCTGAAGTTT
AACTTGGAATGTCTCCACAAGACCTTCGGCCCTGGAGGCCTCCAAGGGGACACGCTGATT
GACATTGGCTCAGGTCCTACCATCTACCAAGTTCTTGCTGCCTGTGATTCCTTCCAAGAC
ATCACTCTCTCCGACTTTACCGACCGCAACCGGGAGGAGCTGGAAAAGTGGCTGAAGAAG
GAGCCGGGGGCCTATGACTGGACCCCAGCGGTGAAATTCGCCTGTGAGCTGGAAGGAAAC
AGCGGCCGATGGGAGGAGAAGGAGGAGAAGCTGCGGGCAGCGGTGAAGCGGGTGCTCAAG
TGCGATGTCCACCTGGGCAACCCGCTGGCCCCGGCTGTGTTGCCTCTCGCCGACTGTGTG
CTCACCCTGCTGGCCATGGAGTGTGCCTGCTGTAGCCTTGATGCCTACCGCGCTGCCCTG
TGCAACCTTGCCTCACTGCTCAAGCCGGGTGGCCACCTGGTGACCACTGTCACGCTTCGG
CTCCCGTCCTACATGGTGGGGAAGCGTGAATTTTCCTGCGTGGCCCTGGAGAAAGAGGAG
GTGGAGCAGGCTGTCCTGGATGCTGGCTTTGACATTGAACAGCTCCTACACAGTCCCCAG
AGCTACTCTGTCACCAATGCTGCCAACAATGGGGTCTGCTTCATTGTGGCTCGCAAGAAG
CCTGGGCCCTGA
|
| Enzyme 5 GenBank Gene ID |
NM_006774.4  |
| Enzyme 5 GeneCard ID |
INMT  |
| Enzyme 5 GenAtlas ID |
INMT  |
| Enzyme 5 HGNC ID |
HGNC:6069  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7p15.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Thompson MA, Moon E, Kim UJ, Xu J, Siciliano MJ, Weinshilboum RM: Human indolethylamine N-methyltransferase: cDNA cloning and expression, gene cloning, and chromosomal localization. Genomics. 1999 Nov 1;61(3):285-97. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [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
]
- Kitano T, Liu YH, Ueda S, Saitou N: Human-specific amino acid changes found in 103 protein-coding genes. Mol Biol Evol. 2004 May;21(5):936-44. Epub 2004 Mar 10. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5655 |
| Enzyme 6 Name |
S-adenosylmethionine synthase isoform type-1 |
| Enzyme 6 Synonyms |
- AdoMet synthase 1
- Methionine adenosyltransferase 1
- MAT 1
- Methionine adenosyltransferase I/III
- MAT-I/III
|
| Enzyme 6 Gene Name |
MAT1A |
| Enzyme 6 Protein Sequence |
>S-adenosylmethionine synthase isoform type-1
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
|
| Enzyme 6 Number of Residues |
395 |
| Enzyme 6 Molecular Weight |
43647.6 |
| Enzyme 6 Theoretical pI |
6.24 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- methionine adenosyltransferase activity
- nucleoside binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- cellular metabolic process
- metabolic process
- one-carbon metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in methionine adenosyltransferase activity |
| Enzyme 6 Specific Function |
Catalyzes the formation of S-adenosylmethionine from methionine and ATP |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine [RN:R00177]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
55959182  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q00266  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
METK1_HUMAN  |
| Enzyme 6 PDB ID |
1O9T  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1188 bp
ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCTACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGGCGGCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTAGACCGCTCAGCTGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGATTTGGACTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
|
| Enzyme 6 GenBank Gene ID |
AL359195  |
| Enzyme 6 GeneCard ID |
MAT1A  |
| Enzyme 6 GenAtlas ID |
MAT1A  |
| Enzyme 6 HGNC ID |
HGNC:6903  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
10q22 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed
]
- Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [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
]
- Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5831 |
| Enzyme 7 Name |
Betaine--homocysteine S-methyltransferase 1 |
| Enzyme 7 Synonyms |
Not Available |
| Enzyme 7 Gene Name |
BHMT |
| Enzyme 7 Protein Sequence |
>Betaine--homocysteine S-methyltransferase 1
MPPVGGKKAKKGILERLNAGEIVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLH
REFLRAGSNVMQTFTFYASEDKLENRGNYVLEKISGQEVNEAACDIARQVADEGDALVAG
GVSQTPSYLSCKSETEVKKVFLQQLEVFMKKNVDFLIAEYFEHVEEAVWAVETLIASGKP
VAATMCIGPEGDLHGVPPGECAVRLVKAGASIIGVNCHFDPTISLKTVKLMKEGLEAARL
KAHLMSQPLAYHTPDCNKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCC
GFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWVRARARKEYWENLRIASG
RPYNPSMSKPDGWGVTKGTAELMQQKEATTEQQLKELFEKQKFKSQ
|
| Enzyme 7 Number of Residues |
406 |
| Enzyme 7 Molecular Weight |
44998.2 |
| Enzyme 7 Theoretical pI |
7.04 |
| Enzyme 7 GO Classification |
| Function |
- S-methyltransferase activity
- betaine-homocysteine S-methyltransferase activity
- binding
- catalytic activity
- cation binding
- homocysteine S-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- methionine biosynthetic process
- sulfur amino acid biosynthetic process
- sulfur amino acid metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 7 General Function |
Involved in zinc ion binding |
| Enzyme 7 Specific Function |
Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline |
| Enzyme 7 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Methionine Metabolism (map00271
)
|
| Enzyme 7 Reactions |
- trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
4530461  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q93088  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
BHMT1_HUMAN  |
| Enzyme 7 PDB ID |
1LT8  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1221 bp
ATGCCACCCGTTGGGGGCAAAAAGGCCAAGAAGGGCATCCTAGAACGTTTAAATGCTGGA
GAGATTGTGATTGGAGATGGAGGGTTTGTCTTTGCACTGGAGAAGAGGGGCTACGTAAAG
GCAGGACCCTGGACTCCTGAAGCTGCTGTGGAGCACCCAGAAGCAGTTCGCCAGCTTCAT
CGAGAGTTCCTCAGAGCTGGCTCAAACGTCATGCAGACCTTCACCTTCTATGCGAGTGAA
GACAAGCTGGAGAACAGGGGCAACTATGTCTTAGAGAAGATATCTGGGCAGGAAGTCAAT
GAAGCTGCTTGCGACATCGCCCGACAAGTGGCTGATGAAGGAGATGCTTTGGTAGCAGGA
GGAGTGAGTCAGACACCTTCATACCTTAGCTGCAAGAGTGAAACTGAAGTCAAAAAAGTA
TTTCTGCAACAGTTAGAGGTCTTTATGAAGAAGAACGTGGACTTCTTGATTGCAGAGTAT
TTTGAACACGTTGAAGAAGCTGTGTGGGCAGTTGAAACCTTGATAGCATCCGGTAAACCT
GTGGCAGCAACCATGTGCATTGGCCCAGAAGGAGATTTGCATGGCGTGCCCCCCGGCGAG
TGTGCAGTGCGCCTGGTGAAAGCAGGAGCATCCATCATTGGTGTGAACTGCCACTTTGAC
CCCACCATTAGTTTAAAAACAGTGAAGCTCATGAAGGAGGGCTTGGAGGCTGCCCGACTG
AAAGCTCACCTGATGAGCCAGCCCTTGGCTTACCACACTCCTGACTGCAACAAGCAGGGA
TTCATCGATCTCCCAGAATTCCCATTTGGACTGGAACCCAGAGTTGCCACCAGATGGGAT
ATTCAAAAATACGCCAGAGAGGCCTACAACCTGGGGGTCAGGTACATTGGCGGGTGCTGT
GGATTTGAGCCCTACCACATCAGGGCAATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTT
TTGCCACCAGCTTCAGAAAAACATGGCAGCTGGGGAAGTGGTTTGGACATGCACACCAAA
CCCTGGGTTAGAGCAAGGGCCAGGAAGGAATACTGGGAGAATCTTCGGATAGCCTCAGGC
CGGCCATACAACCCTTCAATGTCAAAGCCAGATGGCTGGGGAGTGACCAAAGGAACAGCC
GAGCTGATGCAGCAGAAAGAAGCCACAACTGAGCAGCAGCTGAAAGAGCTCTTTGAAAAA
CAAAAATTCAAATCACAGTAG
|
| Enzyme 7 GenBank Gene ID |
AF118378  |
| Enzyme 7 GeneCard ID |
BHMT  |
| Enzyme 7 GenAtlas ID |
BHMT  |
| Enzyme 7 HGNC ID |
HGNC:1047  |
| Enzyme 7 Chromosome Location |
5 |
| Enzyme 7 Locus |
5q13.1-q15 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Garrow TA: Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J Biol Chem. 1996 Sep 13;271(37):22831-8. [PubMed
]
- Park EI, Garrow TA: Interaction between dietary methionine and methyl donor intake on rat liver betaine-homocysteine methyltransferase gene expression and organization of the human gene. J Biol Chem. 1999 Mar 19;274(12):7816-24. [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
]
- Sunden SL, Renduchintala MS, Park EI, Miklasz SD, Garrow TA: Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene. Arch Biochem Biophys. 1997 Sep 1;345(1):171-4. [PubMed
]
- Millian NS, Garrow TA: Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch Biochem Biophys. 1998 Aug 1;356(1):93-8. [PubMed
]
- Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML: Betaine-homocysteine methyltransferase: zinc in a distorted barrel. Structure. 2002 Sep;10(9):1159-71. [PubMed
]
- Weisberg IS, Park E, Ballman KV, Berger P, Nunn M, Suh DS, Breksa AP 3rd, Garrow TA, Rozen R: Investigations of a common genetic variant in betaine-homocysteine methyltransferase (BHMT) in coronary artery disease. Atherosclerosis. 2003 Apr;167(2):205-14. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5895 |
| Enzyme 8 Name |
Methionyl-tRNA synthetase, cytoplasmic |
| Enzyme 8 Synonyms |
- Methionine--tRNA ligase
- MetRS
|
| Enzyme 8 Gene Name |
MARS |
| Enzyme 8 Protein Sequence |
>Methionyl-tRNA synthetase, cytoplasmic
MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLF
STSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRA
LTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQE
PCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAW
EKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRL
RQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTP
QQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDK
CGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQF
ITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWW
KNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGV
GVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMF
VSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQ
VNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSI
LLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQ
QIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK
|
| Enzyme 8 Number of Residues |
900 |
| Enzyme 8 Molecular Weight |
101114.9 |
| Enzyme 8 Theoretical pI |
6.05 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- methionine-tRNA ligase activity
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- methionyl-tRNA aminoacylation
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 8 General Function |
Involved in nucleotide binding |
| Enzyme 8 Specific Function |
ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met) |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet [RN:R03659]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
1702932  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P56192  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
SYMC_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2703 bp
ATGAGACTGTTCGTGAGTGATGGCGTCCCGGGTTGCTTGCCGGTGCTGGCCGCCGCCGGG
AGAGCCCGGGGCAGAGCAGAGGTGCTGATCAGCACTGTAGGCCCGGAAGATTGTGTGGTC
CCGTTCCTGACCCGGCCTAAGGTCCCTGTCTTGCAGGTGGATAGCGGCAACTACCTCTTC
TCCACTAGTGCAATCTGCCGATATTTTTTTTTGTTATCTGGCTGGGAGCAAGATGACCTC
ACTAACCAGTGGCTGGAATGGGAAGCGACAGAGCTGCAGCCAGCTTTGTCTGCTCCCCTG
TACTATTTAGTGGTCCAAGGCAAGAAGGGGGAAGATGTTCTTGGTTCAGTGCGGAGAGCC
CTGACTCACATTGACCACAGCTTGAGTCGTCAGAACTGTCCTTTCCTGGCTGGGGAGACA
GAATCTCTAGCCGACATTGTTTTGTGGGGAGCCCAATACCCATTACTGCAAGATCCCGCC
TACCTCCCTGAGGAGCTGAGTGCCCTGCACAGCTGGTTCCAGACACTGAGTACCCAGGAA
CCATGTCAGCGAGCTGCAGAGACTGTACTGAAACAGCAAGGTGTCCTGGCTCTCCGGCCT
TACCTCCAAAAGCAGCCCCAGCCCAGCCCCGCTGAGGGAAGGGCTGTCACCAATGAGCCT
GAGGAGGAGGAGCTGGCTACCCTATCTGAGGAGGAGATTGCTATGGCTGTTACTGCTTGG
GAGAAGGGCCTAGAAAGTTTGCCCCCGCTGCGGCCCCAGCAGAATCCAGTGTTGCCTGTG
GCTGGAGAAAGGAATGTGCTCATCACCAGTGCCCTCCCTTACGTCAACAATGTCCCCCAC
CTTGGGAACATCATTGGTTGTGTGCTCAGTGCCGATGTCTTTGCCAGGTACTCTCGCCTC
CGCCAGTGGAACACCCTCTATCTGTGTGGGACAGATGAGTATGGTACAGCAACAGAGACC
AAGGCTCTGGAGGAGGGACTAACCCCCCAGGAGATCTGCGACAAGTACCACATCATCCAT
GCTGACATCTACCGCTGGTTTAACATTTCGTTTGATATTTTTGGTCGCACCACCACTCCA
CAGCAGACCAAAATCACCCAGGACATTTTCCAGCAGTTGCTGAAACGAGGTTTTGTGCTG
CAAGATACTGTGGAGCAACTGCGATGTGAGCACTGTGCTCGCTTCCTGGCTGACCGCTTC
GTGGAGGGCGTGTGTCCCTTCTGTGGCTATGAGGAGGCTCGGGGTGACCAGTGTGACAAG
TGTGGCAAGCTCATCAATGCTGTCGAGCTTAAGAAGCCTCAGTGTAAAGTCTGCCGATCA
TGCCCTGTGGTGCAGTCGAGCCAGCACCTGTTTCTGGACCTGCCTAAGCTGGAGAAGCGA
CTGGAGGAGTGGTTGGGGAGGACATTGCCTGGCAGTGACTGGACACCCAATGCCCAGTTT
ATCACCCGTTCTTGGCTTCGGGATGGCCTCAAGCCACGCTGCATAACCCGAGACCTCAAA
TGGGGAACCCCTGTACCCTTAGAAGGTTTTGAAGACAAGGTATTCTATGTCTGGTTTGAT
GCCACTATTGGCTATCTGTCCATCACAGCCAACTACACAGACCAGTGGGAGAGATGGTGG
AAGAACCCAGAGCAAGTGGACCTGTATCAGTTCATGGCCAAAGACAATGTTCCTTTCCAT
AGCTTAGTCTTTCCTTGCTCAGCCCTAGGAGCTGAGGATAACTATACCTTGGTCAGCCAC
CTCATTGCTACAGAGTACCTGAACTATGAGGATGGGAAATTCTCTAAGAGCCGCGGTGTG
GGAGTGTTTGGGGACATGGCCCAGGACACGGGGATCCCTGCTGACATCTGGCGCTTCTAT
CTGCTGTACATTCGGCCTGAGGGCCAGGACAGTGCTTTCTCCTGGACGGACCTGCTGCTG
AAGAATAATTCTGAGCTGCTTAACAACCTGGGCAACTTCATCAACAGAGCTGGGATGTTT
GTGTCTAAGTTCTTTGGGGGCTATGTGCCTGAGATGGTGCTCACCCCTGATGATCAGCGC
CTGCTGGGCCATGTCACCCTGGAGCTCCAGCACTATCACCAGCTACTTGAGAAGGTTCGG
ATCCGGGATGCCTTGCGCAGTATCCTCACCATATCTCGACATGGCAACCAATATATTCAG
GTGAATGAGCCCTGGAAGCGGATTAAAGGCAGTGAGGCTGACAGGCAACGGGCAGGAACA
GTGACTGGCTTGGCAGTGAATATAGCTGCCTTGCTCTCTGTCATGCTTCAGCCTTACATG
CCCACGGTTAGTGCCACAATCCAGGCCCAGCTGCAGCTCCCACCTCCAGCCTGCAGTATC
CTGCTGACAAACTTCCTGTGTACCTTACCAGCAGGACACCAGATTGGCACAGTCAGTCCC
TTGTTCCAAAAATTGGAAAATGACCAGATTGAAAGTTTAAGGCAGCGCTTTGGAGGGGGC
CAGGCAAAAACGTCCCCGAAGCCAGCAGTTGTAGAGACTGTTACAACAGCCAAGCCACAG
CAGATACAAGCGCTGATGGATGAAGTGACAAAACAAGGAAACATTGTCCGAGAACTGAAA
GCACAAAAGGCAGACAAGAACGAGGTTGCTGCGGAGGTGGCGAAACTCTTGGATCTAAAG
AAACAGTTGGCTGTAGCTGAGGGGAAACCCCCTGAAGCCCCTAAAGGCAAGAAGAAAAAG
TAA
|
| Enzyme 8 GenBank Gene ID |
X94754  |
| Enzyme 8 GeneCard ID |
MARS  |
| Enzyme 8 GenAtlas ID |
MARS  |
| Enzyme 8 HGNC ID |
HGNC:6898  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
12q13.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Lage H, Dietel M: Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. Gene. 1996 Oct 31;178(1-2):187-9. [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
]
- 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
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
9553 |
| Enzyme 9 Name |
Methionine adenosyltransferase 2 subunit beta |
| Enzyme 9 Synonyms |
- DTDP-4-keto-6-deoxy-D-glucose 4-reductase
- Methionine adenosyltransferase II beta
- MAT II beta
|
| Enzyme 9 Gene Name |
MAT2B |
| Enzyme 9 Protein Sequence |
>Methionine adenosyltransferase 2 subunit beta
MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGF
RRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNL
AKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVL
RIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRML
DPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKL
ETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH
|
| Enzyme 9 Number of Residues |
334 |
| Enzyme 9 Molecular Weight |
37551.5 |
| Enzyme 9 Theoretical pI |
7.39 |
| Enzyme 9 GO Classification |
| Function |
- binding
- catalytic activity
- dTDP-4-dehydrorhamnose reductase activity
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- carbohydrate metabolic process
- cellular polysaccharide biosynthetic process
- extracellular polysaccharide biosynthetic process
- metabolic process
- polysaccharide biosynthetic process
- polysaccharide metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in dTDP-4-dehydrorhamnose reductase activity |
| Enzyme 9 Specific Function |
Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S- adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S- adenosylmethionine inhibition |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9NZL9  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
MAT2B_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1005 bp
ATGGTGGGGAGGGAGAAAGAACTGTCTATACACTTTGTTCCCGGGAGCTGTCGGCTGGTG
GAGGAGGAAGTTAACATCCCTAATAGGAGGGTTCTGGTTACTGGTGCCACTGGGCTTCTT
GGCAGAGCTGTACACAAAGAATTTCAGCAGAATAATTGGCATGCAGTTGGCTGTGGTTTC
AGAAGAGCAAGACCAAAATTTGAACAGGTTAATCTGTTGGATTCTAATGCAGTTCATCAC
ATCATTCATGATTTTCAGCCCCATGTTATAGTACATTGTGCAGCAGAGAGAAGACCAGAT
GTTGTAGAAAATCAGCCAGATGCTGCCTCTCAACTTAATGTGGATGCTTCTGGGAATTTA
GCAAAGGAAGCAGCTGCTGTTGGAGCATTTCTCATCTACATTAGCTCAGATTATGTATTT
GATGGAACAAATCCACCTTACAGAGAGGAAGACATACCAGCTCCCCTAAATTTGTATGGC
AAAACAAAATTAGATGGAGAAAAGGCTGTCCTGGAGAACAATCTAGGAGCTGCTGTTTTG
AGGATTCCTATTCTGTATGGGGAAGTTGAAAAGCTCGAAGAAAGTGCTGTGACTGTTATG
TTTGATAAAGTGCAGTTCAGCAACAAGTCAGCAAACATGGATCACTGGCAGCAGAGGTTC
CCCACACATGTCAAAGATGTGGCCACTGTGTGCCGGCAGCTAGCAGAGAAGAGAATGCTG
GATCCATCAATTAAGGGAACCTTTCACTGGTCTGGCAATGAACAGATGACTAAGTATGAA
ATGGCATGTGCAATTGCAGATGCCTTCAACCTCCCCAGCAGTCACTTAAGACCTATTACT
GACAGCCCTGTCCTAGGAGCACAACGTCCGAGAAATGCTCAGCTTGACTGCTCCAAATTG
GAGACCTTGGGCATTGGCCAACGAACACCATTTCGAATTGGAATCAAAGAATCACTTTGG
CCTTTCCTCATTGACAAGAGATGGAGACAAACGGTCTTTCATTAG
|
| Enzyme 9 GenBank Gene ID |
AF182814  |
| Enzyme 9 GeneCard ID |
MAT2B  |
| Enzyme 9 GenAtlas ID |
MAT2B  |
| Enzyme 9 HGNC ID |
HGNC:6905  |
| Enzyme 9 Chromosome Location |
5 |
| Enzyme 9 Locus |
5q34-q35 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- LeGros HL Jr, Halim AB, Geller AM, Kotb M: Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II). J Biol Chem. 2000 Jan 28;275(4):2359-66. [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
]
- Ohira M, Morohashi A, Nakamura Y, Isogai E, Furuya K, Hamano S, Machida T, Aoyama M, Fukumura M, Miyazaki K, Suzuki Y, Sugano S, Hirato J, Nakagawara A: Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma. Cancer Lett. 2003 Jul 18;197(1-2):63-8. [PubMed
]
- 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
]
- 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
]
- 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
]
- LeGros L, Halim AB, Chamberlin ME, Geller A, Kotb M: Regulation of the human MAT2B gene encoding the regulatory beta subunit of methionine adenosyltransferase, MAT II. J Biol Chem. 2001 Jul 6;276(27):24918-24. Epub 2001 May 3. [PubMed
]
- Martinez-Chantar ML, Garcia-Trevijano ER, Latasa MU, Martin-Duce A, Fortes P, Caballeria J, Avila MA, Mato JM: Methionine adenosyltransferase II beta subunit gene expression provides a proliferative advantage in human hepatoma. Gastroenterology. 2003 Apr;124(4):940-8. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |