ID   MOCOS_CHAGB             Reviewed;         778 AA.
AC   Q2HE65;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=hxB {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=CHGG_01489;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408029; EAQ93254.1; -; Genomic_DNA.
DR   RefSeq; XP_001220710.1; XM_001220709.1.
DR   AlphaFoldDB; Q2HE65; -.
DR   SMR; Q2HE65; -.
DR   STRING; 38033.XP_001220710.1; -.
DR   EnsemblFungi; EAQ93254; EAQ93254; CHGG_01489.
DR   GeneID; 4388218; -.
DR   eggNOG; KOG2142; Eukaryota.
DR   HOGENOM; CLU_010913_0_0_1; -.
DR   InParanoid; Q2HE65; -.
DR   OMA; WCLVHQG; -.
DR   OrthoDB; 394559at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IEA:UniProtKB-UniRule.
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   Gene3D; 3.40.640.10; -; 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   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 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..778
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000369383"
FT   DOMAIN          651..778
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   REGION          576..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         235
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   778 AA;  85612 MW;  E731233A4CFA3E7B CRC64;
     MARTDDQAKS VDTRYNARVE SLRDKEYPML NGSIYLDHAG TTPYPKSLMD RFAKEMTSNL
     FGNPHSASAS SQLSTARIED IRLRVLRFFN ADPAEFDLVF VANATAGIKL VADALRTAPD
     GFDYSYHQAS HTSLIGVREE ARNSLCLDDQ EVDDWLGGGC PFENDSEDRP VLFAYPAQSN
     MDGRRYPLNW AEKVCRGGTR KTYTLLDAAA LVCSSPLDLS QANAAPDFTV LSFYKIFGFP
     DLGALIVRRD AEEAFDTRRY FGGGTVDMVV CLKEQWHAPK AQFLHERLED GTLPVHSIIA
     LDAALDVHKQ LFGSMRDVAS HTAFLSAMLY TRLELLRHGN GQSVCVLYSP GPETANNGLS
     SGPVVSFNIR NSQGAWISLA EVEKLATLKG FHIRTGGVCN PGGIASALGL EPWEMRRNFS
     SGFRCGTDLD IMAGKPTGVI RASLGAMSTI SDVDSFVEFI AEFYRDASLS PARTEPVPQP
     HDPSRLRIHS MSIYPIKSCC GFQVPSGTDW EVRPEGLAWD REWCLVHQGT GQALSQKRHS
     KMALIRPALD FERGQLRVSY AGELPAHQPR EISIPLSKNP SLFRSSSSRS RSSRVCGEEI
     QAQTYSSTAI NSFFSDVLGV PCLLARFPAG GHGKSMRHSK AHLQKHQLSL LPTARPALPG
     SFPPSPPDSD TEKTVSRRIL LSNESPILAI TLPSVTELNR EIHLSKPGLK EVSPAVFRAN
     IVMTPADPDV PLAPYAEDSW SGIKVGPQQH EFEMLGACRR CHMVCINQET AERARSRL