ID A0A2D3V0W9_9PEZI Unreviewed; 791 AA.
AC A0A2D3V0W9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=RCC_04151 {ECO:0000313|EMBL:CZT18307.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT18307.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT18307.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT18307.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) 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}.
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DR EMBL; FJUY01000005; CZT18307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D3V0W9; -.
DR STRING; 112498.A0A2D3V0W9; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000225277; 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:UP000225277};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 629..791
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 398
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 791 AA; 86796 MW; A19EA12213827E84 CRC64;
MAGEKLTSTM RGTEYDSHIS LMRRKEYPSM FQHAGEALYL DHAGTTPPSA TLLSSFHTDM
LANLYGNPHS TSPSSMRSTQ VIESVRVQAL NFVGADPEMF DLVFTSNTTA AIKLVMEAMR
EQKGGFWFGY HVDSHTSVVG VREAAREHRC FESDSEVDEW SRGSLGGIGL FSYPAQSNLN
GRRLPLTWPA RIRGSDEERK LYTLLDAAAF AATSPLRLGE MEAAPDFTVL SFTKIFGFPD
LGALIVRKDA GHIFRGRRYF GGGTVDMVVC VKEQWHAVKS GSLHEQLEDG TLPFHSILAL
ESAFSSHEQL FGSLSCVAAH TSAIAQELYQ RMLMLRHRNG NPVCRIYKDS RSTYGSGSTQ
GPTLAFNLLD SDGEWISNND VEKLATVKNI HLRTGGLCNP GGVAKHLGLA PWEMRENFSS
GWRCGGGDDI INGRPTGVIR VSFGAMSTSS DAARFADFLN EFFADRSSPV CSSALPSPML
VEDGSPRFYV ESLTIYPIKS CAGWNVPSDT NWDIRREGLI WDREWCVVKT GTGAALSQKA
HPKMALIRPV LDFRAGLLRV RLVGSEDEVT VPLSKDPRHF ATKDYKSCDA TVCGENIVAK
VYTSPAIAGF FTRAIGVSCT LARFPASTST ATDVRHSKGH LRRSGTEQAR RPILLSNESP
ILTISHSSLN RLNETIKAAG GKAVPLAAFR ANIVLAESPF LSPGQEQPWK EDSWEGMRSS
SGTEFAFLGG CRRCQMVCVD QESGEKKQEP FVSLAKTRRF PGGRILFGVH TALARDDEGG
KIRVGEEMKT W
//
