ID A0A2B7XNZ1_9EURO Unreviewed; 863 AA.
AC A0A2B7XNZ1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=GX51_00012 {ECO:0000313|EMBL:PGH10257.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH10257.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGH10257.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGH10257.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH10257.1}.
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DR EMBL; PDNC01000001; PGH10257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XNZ1; -.
DR STRING; 2060905.A0A2B7XNZ1; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000224080; 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:UP000224080};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050, ECO:0000313|EMBL:PGH10257.1}.
FT DOMAIN 668..858
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 863 AA; 96177 MW; 85DC7AA16806574A CRC64;
MTGQLLRPLP NGQPRPVRQQ GSFYPDRIED IREREYPSLK KTTYLDHAGT TLYAASLIDA
FSQEMKANLF GNPHSASSSS QLSTRRVDDA RLRVLRFFKA SPDDFDVVFV ANATAGIKLV
ADALRDYDES GFWYGYHRDA HTSLVGVREL AARGRRCFTD DEEVEQWISQ QIASNMRGRA
SVPTLFAYPA QSNMNGRRLP LDWCRKLRTC NIYSLLDAAS LVSTSPLDLS DPNSAPDFTV
LSFYKIFGFP DLGALIVRKG SHEIFNRRRY FGGGTVGMVT SLEDQWHAKK STSIHDQLED
GTLPFHNIIA LHSAFDVHER LYGSMENISL HTSLLAKTLY DGLVAKRHVN GAGVCEMYKH
KTSSYDDRTT QGPIVSFNMR NRNGEWVGKS EVEKLAAVKN IQIRSGTLCN PGGMTYHLGL
KAEEMKRNYN AGQRCGDDND VIEGKPTGGL RVSLGAMSSV GDVNRFLEFI DEFYVDKSNS
STFTTPQAVT QSQKPSTSKF YVDKLCVYPI KSCGAFIVPD GKEWEIKPEG LAWDREWCLM
HQGTGVALNQ KRYPRMALIR PVIDLDRGVL HISRGMPGTD NNSLELPLSG QSVDFSTAEL
CENSMKKSSM VCGDRVTVQV YSSPVVSRFF SEFLEVPCTL ARFPANSSVR YSKSLPRYRP
AETIYPSNSM PGAFPQSTSS FDQYKNPIRL SNESPMLLIS RSSVNKLNET IKSLGKSASK
TTRAVAADVF RANIIVAENP SLLLNNKNED SNNATPGPIF SPPTLLAEQP YVEDRWAGFR
IGSYKFDVLG SCQRCQMVCV DQFTAVKSEE PFSTLAKTRK IGGKVIFGRH VCLSSDDFWD
GEDGGKVMIR SGQVVEPFYE ESL
//
