ID   MOCOS_CAEBR             Reviewed;         707 AA.
AC   A8X493;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 3.
DT   25-MAY-2022, entry version 66.
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; ORFNames=CBG07703;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP27453.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; HE601041; CAP27453.2; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A8X493; -.
DR   SMR; A8X493; -.
DR   WormBase; CBG07703; CBP37952; WBGene00029667; Cbr-mocs-1.
DR   InParanoid; A8X493; -.
DR   OrthoDB; 394559at2759; -.
DR   Proteomes; UP000008549; 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: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..707
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000369363"
FT   DOMAIN          558..705
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   ACT_SITE        365
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   707 AA;  79290 MW;  49C0D3A2A28CE72E CRC64;
     MPYLDHAGST LPSKTQLEEL AKLQTQLILA NPHSHHSTAI KTQQIVSSAR HRILRYFNTT
     ADDYFVVFTN NTTHALKIVA ENFNFGHRTQ EGVVSEISAV LKGGPSNFAY FNDSHHSVVG
     LRHVVLGKVD AISCVNEDVV KEECIPKVEN SLFVFTAMSN FLIPFQINEK LISGWSVCVD
     AAALVSGTRL DLTAHRPNFV AFSFYKIFGY PTGIGALLVK KDSSKSIEKT SFAGGTVQSV
     DEMTMHFVIR DFERAYEEGT INSYGIAQLQ KGFEEIERCG GMQAIRAHTY DLRSKAVQIL
     QSKTHPNGKK VVEIYSQPHI QVSPETQGAI VAFNLVRPDN GYYGYTEVEK MCAIFGIELR
     TGCFCNIGAC KKYLGITSEM IKENMSKGKR CGDEIDLING RPTGAVRISF GRMSTEQDIE
     VLKQMIDTCF VSSEKVFSPS LQSLKIDSFL PTVVNLFSFP IKSVGSVAKS RYELTPRGFK
     HDREFLVVKD DVTLNLKMHP ELCRLTATIV NDEELHIQTF DQNDNLVIPM SLSLKENDAK
     VVCKKTIATF DCGDKVGQWL ENALDMTNCR LLRVAGESKK NFVNDSPFLL INEASVYMLA
     RHIDMDVQDI LTRFRSNIVV RGLPPFIEDT AKRLSIENLE FEVVDKCTRC EMICVDPMTG
     EKDPSLLLAL RDYRNKQKMT FGIYIRQSNF EPGQFVEAGS AVRFFTD