MOCOS_CAEEL
ID MOCOS_CAEEL Reviewed; 709 AA.
AC Q21657;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
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};
GN Name=mocs-1 {ECO:0000312|WormBase:R03A10.3};
GN ORFNames=R03A10.3 {ECO:0000312|WormBase:R03A10.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z69793; CAA93672.2; -; Genomic_DNA.
DR PIR; T23860; T23860.
DR RefSeq; NP_510552.2; NM_078151.2.
DR AlphaFoldDB; Q21657; -.
DR SMR; Q21657; -.
DR STRING; 6239.R03A10.3; -.
DR PaxDb; Q21657; -.
DR EnsemblMetazoa; R03A10.3.1; R03A10.3.1; WBGene00010983.
DR GeneID; 187534; -.
DR KEGG; cel:CELE_R03A10.3; -.
DR UCSC; R03A10.3; c. elegans.
DR CTD; 187534; -.
DR WormBase; R03A10.3; CE30560; WBGene00010983; mocs-1.
DR eggNOG; KOG2142; Eukaryota.
DR eggNOG; KOG2362; Eukaryota.
DR GeneTree; ENSGT00940000157051; -.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q21657; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; Q21657; -.
DR Reactome; R-CEL-947581; Molybdenum cofactor biosynthesis.
DR PRO; PR:Q21657; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00010983; Expressed in embryo and 2 other tissues.
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:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB.
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; 1.
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; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..709
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000249954"
FT DOMAIN 563..707
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 367
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 709 AA; 79723 MW; 8A0FD2B23634A0A1 CRC64;
MPYLDHAGST LPSKIQLEEV AKQQSQLILA NPHSHHATAV KTKQIVNSAR LRILQYFNTT
SDDYFVVLTN NTTHGLKIVA ENFKFGQKTH SILNIASVLH GGSSNLGYLY DSHHSVVGLR
HVVNGKVNSI SCVNEESILE HEIPDVEHSL FVLTAMSNFC GKKYSLESVH RLQEKGWAVC
LDAASFVSSS ALDLSQQRPN FIAFSFYKIF GYPTGIGALL VRKDSAHLIE KTSFAGGTVQ
SVDEMSMFFV LREFERAFEE GTLNYYGIAQ LQKGFEEIER CGGISSIRNL THHLCKNALY
MLKSKKHPNG RPVVEIYSQS EQFENPDKQG PIVAFNLKRP DGGYYGYTEV EKMCAIFGIE
LRTGCFCNIG ACKKYLGITS EMIQENMSKG KRCGDEIDLI NGTPTGAIRI SFGRTSTEHD
ITALEQMIDT CFTEGEHQAQ SKPDPMNIES YSPTVVNLFS FPIKSVGSVG RKRYELTARG
FKNDREFLIV NDDVTLNLKT HPELCMLTAT IVDDDQLLIQ TFDQNENLVL PMSLSLKDNG
AKLVCKNTIA TMDCGDKVGK WLDNALDRQN CRLLRVAEDS KKNFVNDSPF LLINEASVYM
LSRYINMEVR EILTRFRSNI VVRGLPPFIE DTAKRLSIEN LEFEVVDKCT RCEMICVDPM
TGEKDPSLLL ALRDYRNKQK MTFGIYIRQT NFESGQYLES GMSVNFSTD
