MOCOS_DROYA
ID MOCOS_DROYA Reviewed; 780 AA.
AC B4PYH5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein maroon-like {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=Ma-l {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=mal {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=GE17883;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC 1 sulfur atom in active form. {ECO:0000255|HAMAP-Rule:MF_03050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03050}.
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DR EMBL; CM000162; EDX03016.1; -; Genomic_DNA.
DR RefSeq; XP_002101908.1; XM_002101872.2.
DR AlphaFoldDB; B4PYH5; -.
DR SMR; B4PYH5; -.
DR STRING; 7245.FBpp0262893; -.
DR EnsemblMetazoa; FBtr0264401; FBpp0262893; FBgn0235321.
DR GeneID; 6526091; -.
DR KEGG; dya:Dyak_GE17883; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; B4PYH5; -.
DR Proteomes; UP000002282; Chromosome X.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS:UniProtKB.
DR GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:EnsemblMetazoa.
DR GO; GO:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IEA:EnsemblMetazoa.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_03050; MOCOS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR028886; MoCo_sulfurase.
DR InterPro; IPR005303; MOSC_N.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF00266; Aminotran_5; 2.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..780
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369377"
FT DOMAIN 635..780
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 413
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 246
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 780 AA; 87973 MW; EB7D99BD56BA74C4 CRC64;
MAPYRPEFSA AEQSRIDAEF SRLARNKSVY LDHAGTTLYA ENQVTAAAEQ LQRNVICNPH
TCRLTGDFVD QVRFKILEFF NTTAEDYHVI FTANATAALS LVAENFDFGS TGDFHFCQEN
HTSVLGMRER VRANGIYMLK EKEISGGELK KNGTVHKVSG KTGNSLLTFS AQCNFSGYKI
PLDTIEKIQI DGLSKPGKQL WGSLGENKEN THNDYYICLD AASFVATSPL DLKKYRPDYV
CLSFYKIFGY PTGVGALLVS RRGADVFQKR RFFGGGTINY AYPHAMDYQL RETFHQRYED
GTLPFLAIVG LLEGFRTLER LVPKTDEFST MERISRHVFG LAKYLEDQLR QLQHPNGEPL
VELYNKVGYQ DKSRQGGIVA FNVRTESGSF VGFGEIACVA ALHGILLRTG CFCNIGACQY
YLNLDEDAMD TIYKRAGRIC GDYFDLVDGQ PTGAVRVSFG YMTTFQDVEQ LLQMLRSSYL
ATKPLQRIQF IEEQAEQLPP LLKERVQLLR PKLLQMAIYP VKSCAAFKIE LEGSWPLTDQ
GLRYDREWMI VDMNGMALTQ KRCTELCLIR PVIKVDQLEL QFGDNSHFSV PLSLEDQAAD
SAKCVSKVCR QPVEGLDCGD GVAQWLSENL GLEGLRLLRQ SGQRNSSKDQ QKLSLVNQAQ
FLLLNKSSVR SLQFEEPLDE TVDRFRANII IDTGSAFEEL TYKALSIGGI QFQVEGPCQR
CDMICINQRT GERSPETLTT ISRLQKGRMR FGIYITRIPQ DTKELEAKEH MTCGDVVLVE
