ID A0A2B7Z9F7_9EURO Unreviewed; 859 AA.
AC A0A2B7Z9F7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=GX50_07213 {ECO:0000313|EMBL:PGH30021.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH30021.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH30021.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH30021.1,
RC ECO:0000313|Proteomes:UP000226031};
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:PGH30021.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDND01000196; PGH30021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Z9F7; -.
DR STRING; 73230.A0A2B7Z9F7; -.
DR VEuPathDB; FungiDB:EMCG_07865; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000226031; 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:UP000226031};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050, ECO:0000313|EMBL:PGH30021.1}.
FT DOMAIN 671..854
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT REGION 649..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 859 AA; 95380 MW; E68C5FB312BB1D7C CRC64;
MKGQLFCPQS NGQLDQVGLR GSYTDQIEDI REREYPSLKE TTYLDHAGTT LYPASLIDAF
SREMKENLFG NPHSASSSSL LSTRRVDDAR LRVLRFFKAS PDDFDVVFVA NATAGIKLVA
DALRDCDEGG FWYGYHVDAH TSLVGVREVA ARGRKCFADD KEVEEWISHQ HASNMRRRTS
VPTLFAYPAQ SNMTGRRLPL DWCRNLRTCN IYSLLDAASL VSTSPLDLSD PDSAPDFTAF
SFYKIFGFPD LGALIVRKGS HNIFDKRRYF GGGTVGMVTS LEDQWHAKKS TSIHDQLEDG
TLPFHSIIAL HSAFDVYERL YGSMENISRH TGALAKTLYD CLSSKRHGNG TIVCEMYKHK
TSSYDDRTTQ GPIVSFNMRN SNGEWIGKSD VEKLAAVKNI QIRSGTLCNP GGMAYHLGLK
IEEMKRNYNA GQRCGDDNDV IEGKPTGGLR VSLGAMSSIG DVNRFLDFID EFYVDKSQSN
TSLTPQSVAQ SERPSPSSFY VDRLCVYPIK SCGAFIVPDG KQWEIKPEGL AWDREWCLMH
QGTGVALNQK RYPRMALIRP VIDLDRGVLQ ISRGMPGTDR SSLELPLSGQ SVDISTAELC
ENSMKKSSMV CGDRVTVQIY SSPAVSAFFS EFLEVPCTLA RFPANSSVRY SKPQPRYRLP
ETNSPSNSMP GAFPQSTPSS QLYKNPIRLS NESPMLLISR SSVNKLNETI KLSGKTTSTG
TKAVAADVFR ANIIVAENPA PVLNTKNKNS NAISTPQNLL AEQPYIEDTW TGFRIGAHKF
DVLGSCQRCQ MVCVDQFTAV RSEEPFSTLA KTRKVSGKVI FGRHVCLSPD LDEGMVRAER
GKVMIKTGEV VEPLYEETF
//
