ID F9XG01_ZYMTI Unreviewed; 793 AA.
AC F9XG01;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=MYCGRDRAFT_74083 {ECO:0000313|EMBL:EGP85709.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP85709.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP85709.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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; CM001202; EGP85709.1; -; Genomic_DNA.
DR RefSeq; XP_003850733.1; XM_003850685.1.
DR AlphaFoldDB; F9XG01; -.
DR STRING; 336722.F9XG01; -.
DR EnsemblFungi; Mycgr3T74083; Mycgr3P74083; Mycgr3G74083.
DR GeneID; 13397851; -.
DR KEGG; ztr:MYCGRDRAFT_74083; -.
DR VEuPathDB; FungiDB:ZTRI_7.418; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_0_1; -.
DR InParanoid; F9XG01; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000008062; Chromosome 7.
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; 3.40.640.10; 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 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:UP000008062};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT DOMAIN 614..790
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT ACT_SITE 394
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 793 AA; 87303 MW; 6BC53FA3B560965C CRC64;
MAATMDLHEY DAYISQMREA EYPMLKGSLY LDHAGTTLYS KTLMDRFHAD MMANLYGNPH
SGAPSSQRST AEIEAVRIQA LEYFGADPDD FDLVFTANTT AAIKLIMEAF RQQRHGFWYG
YHVDSHTSLI GVRESAKDQR CFESDLEVEK WIHNESEMDE AALPRLFGYP AQSNMNGRRL
PLDWDAKSRS GSRRRKVYTL CDAAAYAATT PLRLNELERA PDFTVLSFSK IFGFPDLGAL
IVRKDVAHLF SGRRYFGGGT VDMVVCVKEQ WHAMKSGSLH EQLEDGTLPV HSIIALKSAM
STLKALFRSL DHIAEHTLAL ALQLHQDLKS LQHANGTTAC EIYRGDGSTY ENAATQGPTI
AFNIRNSQGQ YVSNAEIEKL AAIKNIHLRT GGLCNPGGVV KHLKLDPWEM RENFSAGFRC
GSENDILNGK PTGMLRVSFG AMSTRADATR FADFVKEFFI ERGLPSSSPS SPLMIDDGMS
SRLHVESLTV YPIKSCGGWR IPYGTPWDIR PEGLAWDREW CLVKQGNGVV LSQKGHPRMA
LIRPQLEFAA GYLRISISGS TQQITVPLSK DPSYFATPDF RDCSANVCGD TVQARIYTSK
AIADFFTRAI GIPCTLARFP AASSSSPSIR HSKTHLQQIG LLSSTPRPIL LSNESPILTI
SRSSLNRLNE GIKASGGKAA HPAVFRANIV LAGSPILPPG QEQPWAEDSW SSMRIGGEGG
AMFDLLGGCR RCQMVCIDQE SGEKNQEPFV TLAKTRRFNG RVLFGVHTAL ANGGNSGGLS
IKAGDEVQTW LEP
//
