ID   MOCOS_ASPFC             Reviewed;         843 AA.
AC   B0Y691;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=AFUB_066090;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499598; EDP50276.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y691; -.
DR   SMR; B0Y691; -.
DR   EnsemblFungi; EDP50276; EDP50276; AFUB_066090.
DR   VEuPathDB; FungiDB:AFUB_066090; -.
DR   HOGENOM; CLU_010913_0_0_1; -.
DR   PhylomeDB; B0Y691; -.
DR   Proteomes; UP000001699; 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   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; Transferase.
FT   CHAIN           1..843
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000369379"
FT   DOMAIN          657..836
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         241
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   843 AA;  94161 MW;  1109FA5E1C1715BC CRC64;
     MVGVTSCEEE ILEYGRGYSE DVDTIREREY PQLKDTTYLD HAGTTLYAKS LIESFSRELT
     SNLFGNPHSL STSSQLSTQR VDDVRLRALR FFKADPEEFD LVFVANATAA IKLVADGMRD
     STRQGFWYGY HVDAHTSLVG VRELAEKGGR CFTSDDEVED WISRLCDVRS ESLKLFAYPA
     QSNMNGRRLP FSWCKKIRDQ GETTGGNVYT LLDAASLVST SPLDLSDASA APDFTVLSFY
     KIFGFPDLGA LIVRKSAGQI FEHRRYFGGG TVDMVLTRGL QWHAKKQSSI HDRLEDGTLP
     FHNIIALDSA FATHERLFGS MQNISSHTRF LAKRLYDRLN ALRHFNGQRV CELYKSPRSD
     YNQPSTQGPI IAFNLRNSQG SWIGKSEVER LAATKNIQIR SGSLCNPGGT SGSLGWTGAD
     LLQQFSAGLR CGDDHDVMDG RPTGVLRLSL GPMTNLEDIN TFVELVEEFY VEKAATVDSL
     VAPVHSVPLQ QPRFYIESLS LYPIKSCGPF KVPDGRRWEI RREGLAWDRE WCLIHQGTGA
     ALNQKKYPRM ALIRPSIDLD RNVLRVTCGE PGSTDQKLLE VSLLRENTEL ATTSLCQRTS
     KASTVCGDQV TVQAYTSPPV AQFFSDFLGV PCTLARFPPH SSTRYASPRK APGAWKQYLR
     KFVMPGSFPQ DPSPPPAEKH PILLSNESPI LLISRSSVNY LNENIKANQK KIRTGTSKAV
     AADVFRANIV VAESLADSPK MEQPYIEDQW EALKIGPGEL RFDVLGSCQR CSMVCIDQFT
     GVRRDEPFST LAKTRKINNK IVFGRHCSLS ASEVTQDQHD NAERWTLMVG DIVIPSYAHD
     YTL