ID   MOCOS_ASPOR             Reviewed;         822 AA.
AC   Q2UH11;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   25-MAY-2022, entry version 85.
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=AO090023000633;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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=BAE59154.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007157; BAE59154.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001821156.2; XM_001821104.2.
DR   AlphaFoldDB; Q2UH11; -.
DR   SMR; Q2UH11; -.
DR   STRING; 510516.Q2UH11; -.
DR   PRIDE; Q2UH11; -.
DR   EnsemblFungi; BAE59154; BAE59154; AO090023000633.
DR   GeneID; 5993158; -.
DR   KEGG; aor:AO090023000633; -.
DR   VEuPathDB; FungiDB:AO090023000633; -.
DR   Proteomes; UP000006564; Chromosome 3.
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   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   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..822
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000249962"
FT   DOMAIN          643..820
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   REGION          633..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   822 AA;  91162 MW;  846EF95DC0255FFB CRC64;
     MQAKSKTESR AEYCTGYSED VDVIREREYP FLKDTTYLDH AGTTLYPKSL IDSFARDLTS
     NLFGNPHSRS SSSQLSTQRI DDIRLRALRF FNADPDEFDL VFVANATAAI KLVVDVFRDS
     SPQGFWYGYF IDAHTSLVGA REIAERGHRC FLTSGEVERW IADLATDQKN FPRLFAYPGQ
     SNLNGRRSPM QWCKKIRDGS SGAGNVYTLL DAASLVSTSP LDLSDASAAP DFTALSFYKI
     FGFPDLGALI VRKSAAGIIK KRKFFGGGTV DMVLAQGMPW HAKKSTIHEC LEDGTLPFHN
     IIALDSALST HGRLFGSMSN VSFHTRYLAK RLHNRLAAMT HFNGQKVCHL YMSPESDFDN
     STQGPIIAFN IRNSSGAWIG KSEVERLANV KKIHIRSGSH CNSGGTATSL GWTGPELLRN
     FSAGLRCGDD HDVMDGRPTG ILRVSLGAVS NLRDIDAFAR FIDEFYIEKE PEFVSLVPPM
     EVVLQEPSFY VESLSVYPIK SCGAFKVPDG QRWEIKREGL AWDREWCLIH QGTGAALSMK
     KYPRMALIRP VIDLERGVLR ITCGSDSKEL EVSLRREITN LVTTSLCQSA KSSNVCGDRV
     VVQAYSSPTV ASFFSNFLGV PCTLARFPPQ ISTRISNPTR SSRRSQRALM PGSFPEDPSP
     TSEQPPILLS NESPILLISR SSVNRLNENI KYNPRPSYST PAKAVEADVF RANIVVAENL
     HQLANAERPY IEDTWESFSV GPEQLCFDVL GSCQRCQMVC VDPYTGTRRE EPYSTLVKTR
     KINSKIVFGR HTSLSNMELS QGAGKPKSCT VMVGDVVTPQ IA