ID A0A010QXS5_9PEZI Unreviewed; 817 AA.
AC A0A010QXS5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Molybdenum cofactor sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MCS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MOS {ECO:0000256|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase {ECO:0000256|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000256|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_03050};
GN Name=hxB {ECO:0000256|HAMAP-Rule:MF_03050};
GN ORFNames=CFIO01_02220 {ECO:0000313|EMBL:EXF85007.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF85007.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF85007.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF85007.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_03050};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03050};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. MOCOS subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03050}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF85007.1}.
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DR EMBL; JARH01000134; EXF85007.1; -; Genomic_DNA.
DR RefSeq; XP_007591447.1; XM_007591385.1.
DR AlphaFoldDB; A0A010QXS5; -.
DR STRING; 1445577.A0A010QXS5; -.
DR KEGG; cfj:CFIO01_02220; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000020467; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; MOCOS_middle.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 3: Inferred from homology;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_03050};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03050};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 650..816
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 626..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 817 AA; 89876 MW; B94F91E8719EF1F6 CRC64;
MIDADMSSYN SRVDEFRDRE YPMIKDSIYL DHAGTTLYAK SLVDRFSAEL TSNLLGNPHS
ASPSSQYSTS RIEDIRLKLL RFFNADPEEF DLVFVSNTTA GIKLVSDAFR ASPDGFSYVY
HQACHTSIIG VREEARESRC VTDGDVRRWI DGQSPLDDSE ASDSPTLFSY TAQSHMDGRR
YPLTWPSLLR ESPAASHRQF YTLLDAASLV ATSPLDLSNS NTAPDFTVLS LYKIFGFPDL
GALIVRRQAE PIFNQRRYFG GGTVDMVVCG KERWHAPKSA FLHERLEDGT LPFHNIIGLD
AALDVHAELF GSMTCVASHT AFLRNRLYDG LASLKHGNGL PVCTIYSERR SGVNGSVGSG
PVISFNIRDA AGAWISLYEL EKLATLKNLH IRTGGVCSPG GIASALGLSP WEMRKNFSAG
FRCGTDQDII AGKPTGVIRA SLGAMSTISD VDFLIDFIDE FYREEASVDD CRNENQTLSI
GFQVQGISVY PIKSCGGFAV PLGMDWEIMP EGLAWDREWC LVHQGSGQAL SQKRYPKMAL
FKPTLDFGGG VLRVAYRGSK PSHLSDEISV PLSADPTYFE TNGCPRERSS RVCGDKITTQ
VYASDHVNGF FSDILGVPCA LARFPAGGQG QSMRHSKAKV QKHQHPQVWS RKGSFEASPE
LPSPPDSDSE QSPAKILLSN ESPILLINTS SLRALNDEIQ ATGGEPVPSE AFRGNILVGP
TQDSDHLPWA EDGWRKLTIG GEDFTMLGSC RRCQMVCVDQ KSGERHQEPF VTLSKVRRFD
GKVYFGTHMS HDSTTVLLRE GTHRPSIRIG DIVSVGA
//
