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Identification
HMDB Protein ID HMDBP08969
Secondary Accession Numbers
  • 14703
Name Molybdenum cofactor sulfurase
Synonyms
  1. MCS
  2. MOS
  3. MoCo sulfurase
  4. hMCS
Gene Name MOCOS
Protein Type Enzyme
Biological Properties
General Function Involved in metabolic process
Specific Function Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime.
Pathways Not Available
Reactions
Molybdopterin + L-Cysteine + Hydrogen Ion → thio-molybdenum cofactor + L-Alanine + Water details
GO Classification
Biological Process
molybdopterin cofactor biosynthetic process
water-soluble vitamin metabolic process
Mo-molybdopterin cofactor biosynthetic process
Cellular Component
cytosol
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
cofactor binding
pyridoxal phosphate binding
molybdenum ion binding
Molecular Function
Mo-molybdopterin cofactor sulfurase activity
molybdenum ion binding
transferase activity
pyridoxal phosphate binding
Process
metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location 18
Locus 18q12
SNPs MOCOS
Gene Sequence
>2667 bp
ATGGCCGGCGCGGCGGCGGAGTCAGGGCGGGAGCTGTGGACCTTCGCGGGTTCCCGGGAC
CCGAGCGCACCGCGGCTAGCCTACGGCTACGGCCCGGGCAGCCTGCGCGAGCTGCGGGCG
CGCGAGTTCAGCCGCCTGGCAGGAACTGTCTATCTTGACCATGCAGGTGCCACCTTGTTC
TCCCAGAGCCAGCTCGAAAGCTTCACTAGTGATCTCATGGAAAACACTTATGGTAATCCT
CACAGCCAGAACATCAGCAGCAAGCTCACCCATGACACTGTGGAGCAGGTGCGCTACAGA
ATCCTGGCGCACTTCCACACCACCGCAGAAGACTACACTGTGATCTTCACTGCCGGGAGC
ACGGCTGCTCTCAAACTGGTGGCAGAGGCCTTTCCATGGGTGTCCCAGGGCCCAGAGAGC
AGTGGGAGTCGCTTCTGTTACCTCACCGACAGCCACACCTCCGTAGTGGGTATGCGGAAC
GTGACCATGGCTATAAATGTCATATCCACCCCGGTCAGGCCAGAGGACCTGTGGTCTGCA
GAGGAACGTAGTGCTTCAGCCAGCAACCCAGACTGCCAGCTGCCGCATCTCTTCTGCTAC
CCAGCTCAGAGTAACTTTTCTGGAGTCAGATACCCCCTGTCCTGGATAGAAGAGGTCAAG
TCTGGGCGGTTGCACCCTGTGAGCACGCCTGGGAAGTGGTTTGTGCTGCTGGATGCAGCC
TCCTACGTGAGCACCTCGCCTTTGGACCTGTCAGCTCACCAGGCCGACTTTGTCCCCATC
TCCTTCTATAAGATCTTCGGGTTTCCTACAGGCCTGGGCGCTCTGCTGGTCCATAATCGT
GCGGCTCCTCTACTGAGGAAGACCTACTTTGGAGGAGGGACAGCCTCTGCGTACCTAGCA
GGAGAAGACTTCTACATCCCGAGGCAGTCGGTAGCTCAGAGGTTTGAAGATGGCACCATC
TCATTCCTTGATGTTATCGCGCTAAAACATGGATTTGACACCCTAGAGCGCCTCACAGGT
GGAATGGAGAATATAAAGCAGCACACCTTCACCTTGGCTCAGTATACCTACGTGGCCCTG
TCCTCTCTCCAGTACCCCAATGGAGCCCCTGTGGTGCGGATTTACAGCGATTCTGAGTTC
AGCAGCCCTGAGGTTCAGGGCCCAATCATCAATTTTAATGTGCTGGATGACAAAGGGAAC
ATCATTGGTTACTCCCAGGTGGACAAAATGGCCAGTCTTTACAACATCCACCTGCGAACT
GGCTGCTTCTGTAACACTGGGGCCTGCCAGAGGCACCTGGGCATAAGCAACGAGATGGTC
AGGAAGCATTTTCAGGCTGGTCATGTCTGTGGGGACAATATGGACCTCATAGATGGGCAG
CCCACAGGATCTGTGAGGATTTCATTTGGATACATGTCGACGCTGGATGATGTCCAGGCC
TTTCTTAGGTTCATCATAGACACTCGCCTGCACTCATCAGGGGACTGGCCTGTCCCTCAG
GCCCATGCTGACACCGGGGAGACTGGAGCCCCATCAGCAGACAGCCAGGCTGATGTTATA
CCTGCTGTCATGGGCAGACGTAGCCTCTCGCCTCAGGAAGATGCCCTCACAGGCTCCAGG
GTTTGGAACAACTCGTCTACTGTGAATGCTGTGCCTGTGGCCCCACCTGTGTGTGATGTC
GCCAGAACCCAGCCGACTCCTTCAGAGAAAGCTGCAGGAGTCCTGGAGGGGGCCCTTGGG
CCACATGTTGTCACTAACCTTTATCTCTATCCAATCAAATCCTGTGCTGCATTTGAGGTG
ACCAGGTGGCCTGTAGGAAACCAAGGGCTGCTATATGACCGGAGCTGGATGGTTGTGAAT
CACAATGGTGTTTGCCTGAGTCAGAAGCAGGAACCCCGGCTCTGCCTGATCCAGCCCTTC
ATCGACTTGCGGCAAAGGATCATGGTCATCAAAGCCAAAGGGATGGAGCCTATAGAGGTG
CCTCTTGAGGAAAATAGTGAACGGACTCAGATTCGCCAAAGCAGGGTCTGTGCTGACAGA
GTAAGTACTTATGATTGTGGAGAAAAAATTTCAAGCTGGTTGTCAACATTTTTTGGCCGT
CCTTGTCATTTGATCAAACAAAGTTCAAACTCTCAAAGGAATGCAAAGAAGAAACATGGA
AAAGATCAACTTCCTGGTACAATGGCCACCCTTTCTCTGGTGAATGAGGCACAGTATCTG
CTGATCAACACATCCAGTATTTTGGAACTTCACCGGCAACTAAACACCAGTGATGAGAAT
GGAAAGGAGGAATTATTCTCACTGAAGGATCTCAGCTTGCGTTTTCGTGCCAATATTATT
ATCAATGGAAAAAGGGCTTTTGAAGAAGAGAAATGGGATGAGATTTCAATTGGCTCTTTG
CGTTTCCAGGTTTTGGGGCCTTGTCACAGATGCCAGATGATTTGCATCGACCAGCAAACT
GGGCAACGAAACCAGCATGTTTTCCAAAAACTTTCTGAGAGTCGTGAAACAAAGGTGAAC
TTTGGCATGTACCTGATGCATGCATCATTGGATTTATCCTCCCCATGTTTCCTGTCTGTA
GGATCTCAGGTGCTCCCTGTGTTGAAAGAGAATGTGGAAGGTCATGATTTACCTGCATCT
GAGAAACACCAGGATGTTACCTCCTAA
Protein Properties
Number of Residues 888
Molecular Weight 98118.965
Theoretical pI 6.696
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Molybdenum cofactor sulfurase
MAGAAAESGRELWTFAGSRDPSAPRLAYGYGPGSLRELRAREFSRLAGTVYLDHAGATLF
SQSQLESFTSDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHFHTTAEDYTVIFTAGS
TAALKLVAEAFPWVSQGPESSGSRFCYLTDSHTSVVGMRNVTMAINVISTPVRPEDLWSA
EERSASASNPDCQLPHLFCYPAQSNFSGVRYPLSWIEEVKSGRLHPVSTPGKWFVLLDAA
SYVSTSPLDLSAHQADFVPISFYKIFGFPTGLGALLVHNRAAPLLRKTYFGGGTASAYLA
GEDFYIPRQSVAQRFEDGTISFLDVIALKHGFDTLERLTGGMENIKQHTFTLAQYTYVAL
SSLQYPNGAPVVRIYSDSEFSSPEVQGPIINFNVLDDKGNIIGYSQVDKMASLYNIHLRT
GCFCNTGACQRHLGISNEMVRKHFQAGHVCGDNMDLIDGQPTGSVRISFGYMSTLDDVQA
FLRFIIDTRLHSSGDWPVPQAHADTGETGAPSADSQADVIPAVMGRRSLSPQEDALTGSR
VWNNSSTVNAVPVAPPVCDVARTQPTPSEKAAGVLEGALGPHVVTNLYLYPIKSCAAFEV
TRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQRIMVIKAKGMEPIEV
PLEENSERTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRPCHLIKQSSNSQRNAKKKHG
KDQLPGTMATLSLVNEAQYLLINTSSILELHRQLNTSDENGKEELFSLKDLSLRFRANII
INGKRAFEEEKWDEISIGSLRFQVLGPCHRCQMICIDQQTGQRNQHVFQKLSESRETKVN
FGMYLMHASLDLSSPCFLSVGSQVLPVLKENVEGHDLPASEKHQDVTS
GenBank ID Protein 157388923
UniProtKB/Swiss-Prot ID Q96EN8
UniProtKB/Swiss-Prot Entry Name MOCOS_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_017947.2
GeneCard ID MOCOS
GenAtlas ID MOCOS
HGNC ID HGNC:18234
References
General References
  1. 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:15489334 ]
  2. 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. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  4. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  6. Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [PubMed:16177791 ]
  7. Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T: Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. Biochem Biophys Res Commun. 2001 Apr 20;282(5):1194-200. [PubMed:11302742 ]
  8. Yamamoto T, Moriwaki Y, Takahashi S, Tsutsumi Z, Tuneyoshi K, Matsui K, Cheng J, Hada T: Identification of a new point mutation in the human molybdenum cofactor sulferase gene that is responsible for xanthinuria type II. Metabolism. 2003 Nov;52(11):1501-4. [PubMed:14624414 ]
  9. Peretz H, Naamati MS, Levartovsky D, Lagziel A, Shani E, Horn I, Shalev H, Landau D: Identification and characterization of the first mutation (Arg776Cys) in the C-terminal domain of the Human Molybdenum Cofactor Sulfurase (HMCS) associated with type II classical xanthinuria. Mol Genet Metab. 2007 May;91(1):23-9. Epub 2007 Mar 23. [PubMed:17368066 ]