ID A0A1V6RGK6_9EURO Unreviewed; 840 AA.
AC A0A1V6RGK6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=PENSOL_c005G11483 {ECO:0000313|EMBL:OQE00947.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQE00947.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE00947.1}.
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DR EMBL; MDYO01000005; OQE00947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RGK6; -.
DR STRING; 60172.A0A1V6RGK6; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000191612; 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:UP000191612};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 668..836
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 405
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 241
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 840 AA; 93276 MW; 4CD247C1405815E5 CRC64;
MVESTFQGSV HPKYSQGYSA DVDIIRDQEY PLLNGTTYLD YAGTTPYAKS MIESFSRDLT
SNLFGNPHSM SVSSQLSTQR TEDVRVRILR FFNADPDEFD LVFVANATAG IKLVADSLRD
SDHRGFWYGY HIDAHTSIVG VRELAEMGYQ CFQNDDEMEA EITKLAGNQS KAPRLLAYPA
QSNMNGRRLP MRWCEQVRSA TNESGGNVYT LLDAASLVST APLDLGPSSS APDFTVLSFY
KIFGFPDLGA LIVRKSAARV FERRKYFGGG TVDMVLATGV QWHAKKETSI HERLEDGTLP
FHSIIALDTA LDTHERLFGS MANISAHTSF LAKQVYEKLS SLAHFNERKV CQIYQSHTSS
YGNSHAQGPI IAFNLCNSRG EWVPKTEVEK LATVQNMQIR TGSVCNPGGT ASSLGWTGPE
LRRHYSAGLR CGDNHDVLGG RPTGILRVSI GATTNMKDID SLINFIEEFY VEKCPPIVAL
DPLTEDNEVV APHFYVESLA VFPIKSCGAF KIPEGKRWEV KKEGLAWDRE WCLVHQGTGA
ALNQKRYPRM CLIRPSIEIE KGVLRITCGA IAAPDQVSLE ISLGWEDTSL ISTSFCPSST
KKPTTVCGDP ISLHAYTSPV VSAFFSDFLG VPCTLARFPT QTASRYSRMQ RMPNTWKNRF
RKLIMPGSFP PDFPPPARES GQTQITLSNE SPILIVSRSS VNRLNETIKA NTKYGSSKTV
AADVFRGNIV VSERLAHRGD VEQPYAEDRW SSLRIGPDQL RFDALEACQR CQMVCIDQFT
GVRRAEPFST LAKTRNIDGK VKFGKYSALS PEELEGFDSE LPDRRTLMIG DVVVPSYQDD
//
