MOCOS_ASPNC
ID MOCOS_ASPNC Reviewed; 823 AA.
AC A2QIK9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=An04g03890;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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; AM270075; CAK38653.1; -; Genomic_DNA.
DR RefSeq; XP_001401755.1; XM_001401718.2.
DR AlphaFoldDB; A2QIK9; -.
DR SMR; A2QIK9; -.
DR PaxDb; A2QIK9; -.
DR EnsemblFungi; CAK38653; CAK38653; An04g03890.
DR GeneID; 4990795; -.
DR KEGG; ang:ANI_1_1786184; -.
DR VEuPathDB; FungiDB:An04g03890; -.
DR HOGENOM; CLU_010913_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
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..823
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369380"
FT DOMAIN 644..819
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT REGION 628..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 228
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 823 AA; 90996 MW; D1AFCEE21EE93870 CRC64;
MSDRGKCQYP DDVDVIRERE YPLLKDTTYL DHAGTTLYAK SLIESFSRDL TSNLYGNPHS
MSAPSQLSTQ RVDDIRLRAL RFFSADPEEF DLVFVANATA AIKLVADSFR ESTPQGFWYG
YHVDSHTSLV GARELAGIGS RCFVTDAEVE SWISQLDTEP VQGPRLFAYP AQSNMNGRRF
PRGWCGRIRE SAKDTYTLLD VASLVSTSPF DLSDASAAPD FAVLSFYKIF GFPDLGALIV
RKSAGHIFDK RKFFGGGTVD MVLTQGTQWH AKKQSSIHER LEDGTLPFHN IIALGSAFDT
HERLFGSMDN ISSHTRFLAK RLYDRMTTLR HYNGESVCHV YKPSHSDYTD PSTQGPILAF
NLRSSQGAWI GKSEVEKMAS VRNIQIRSGT LCNPGGTAAS LNWSGADMLR HFGAGMRCGD
DHDIMDGRPT GILRVSLGAM SNLTDIDTFM GFIEEFYVEK SPNVCALVPP LEANLTHRSG
FHVESLSVYP IKSCGAFKVP DGKRWEIRRE GLVWDREWCL IHQGTGTALN QKRYPRMALI
RPFIDLSHGV LRVTCGSIRS PSQKTLEIPL DRENSNLTTT SLCQNSSKPS TVCGDQVIVQ
AYSSPTVSAF FSDFLGVPCT LARFPPQSST RLAEPRRGLG SRKSPLRPAM PGAFPQDTPT
PEAERNPILL SNESPILLIS RSSVNRLNET IKSSPTTTNS TGRKKAVAAD VFRANIVVAE
DFPQPVSAGR PYIEDHWESL RIGPDNLHFN VLGSCQRCQM VCVDQLTGVR GEEPYSTLAK
TRKSGNKIYF GRHLAISSNG DGNSVNSRTV MVGDVVTPSY YGP
