MOCOS_ASPCL
ID MOCOS_ASPCL Reviewed; 845 AA.
AC A1CHL0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=ACLA_048350;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027054; EAW10365.1; -; Genomic_DNA.
DR RefSeq; XP_001271791.1; XM_001271790.1.
DR AlphaFoldDB; A1CHL0; -.
DR SMR; A1CHL0; -.
DR STRING; 5057.CADACLAP00004697; -.
DR EnsemblFungi; EAW10365; EAW10365; ACLA_048350.
DR GeneID; 4704171; -.
DR KEGG; act:ACLA_048350; -.
DR VEuPathDB; FungiDB:ACLA_048350; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR Proteomes; UP000006701; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..845
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369378"
FT DOMAIN 666..840
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 404
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 240
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 845 AA; 94023 MW; 100FBA64214CC407 CRC64;
MVGVKTQGED ILEYGRGYSE DVDIIREREY PQLKDTTYLD HAGTTLYAKS LIEAFSRDLT
SNLFGNPHSM SASSQLSTRR VDDVRLRALR FFKADPDDFD LVFVANATAA IKLVADAMRD
SRQGFWYGYH VDAHTSLVGA RELAAKGNRC FSSDEEVEGW IQSLREAGPE SLNLFAYPAQ
SNLNGRRLPL SWCETIRRRS EAAGGNTYTL LDAASLVSTS PLDLSDAAAA PDFTVLSFYK
IFGFPDLGAL IVRKSAGHIF EQRRFFGGGT VDMVLTREMQ WHAKKQSSIH DRLEDGTLPF
HSIIALDSAF ATHRRLFGSM ENVSSHTRFL AKRLYDKLAA LKHSNGERVC QLYTNPFSDY
NKAASQGPII AFNLRNSHGA WIGKSEVERL ATVKNIQFRS GSLCNPGGTS GSLGWTGADL
LQQFSAGLRC GDDHDVMDGR PTGVLRLSLG AMTNLADINT VIQFVEEFYV ERAAAVESLI
TPVPSIPVQQ PRFYIESLSV YPIKSCGAFR VPDGKRWEIR REGLAWDREW CLVHQGTGAT
LNQKKYPRMA LIRPFVDLDR NVLRITCGEL TSSDQQVLEV SLDREDTNLV STSICQRSSK
SSTVCGDQVV VQAYSSPSVS RFFSEFLGVP CTLARFPPQS SSRFSPPKRP SGAWKQYLRK
FVMPGSFPQD SSPSSAPERN PILLSNESPI LLISRSSVNY LNENIKANQK KKKRAEGSSS
SRAVAADVFR ANIVVAESFT QLPRVESPYV EDHWESLKIG PEHLQLDVLG ACQRCSMVCI
DQFTGVRRDE PFSTLAKTRK INGKIVFGRH ASLASSEVTR DEHDTTERWT LMVGDTVTPS
YTHEE
