ID M5WM28_PRUPE Unreviewed; 817 AA.
AC M5WM28;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 ORFNames=PRUPE_4G138400 {ECO:0000313|EMBL:ONI11978.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI11978.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI11978.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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; CM007654; ONI11978.1; -; Genomic_DNA.
DR RefSeq; XP_007213648.1; XM_007213586.1.
DR AlphaFoldDB; M5WM28; -.
DR STRING; 3760.M5WM28; -.
DR EnsemblPlants; ONI11978; ONI11978; PRUPE_4G138400.
DR GeneID; 18780634; -.
DR Gramene; ONI11978; ONI11978; PRUPE_4G138400.
DR KEGG; pper:18780634; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR Proteomes; UP000006882; Chromosome g4.
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; 2.
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:UP000006882};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03050}.
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
FT MOD_RES 271
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03050"
SQ SEQUENCE 817 AA; 90823 MW; A4D815B04E5CF551 CRC64;
MEASKEAFLR EFGEHYGYPN GPKTIDEIRA TEFKRLDGLV YLDHAGATMY SELQMEAIFK
DFTTNVYGNP HSQSDTSSST SDIVREARQQ VLDYCKASPK DYSCIFTSGA TAALKLVGEA
FPWSCQSCFT YTMENHNSVL GIREYALDQG AAAFAIDVEE TVHHGVSNGT AASMKVLQYQ
VQRRNEASSL EEPTGEAYNL FAFPSECNFS GLRFSLDLVK IIKEDPARIL EGSPFCNGRW
MVLIDAAKGS ATEPPDLSLY PADFVVMSFY KLFGYPTGLG VLIARNDASR LLKKTYFSGG
TVATSIADID FVRRRKSVEE LFEDGTISFL SIASVHHGFK ILNSLTVSAI SRHTASLAWY
VRKKLLGLRH ENGARVCTLY GDSKALFHDF GPTVSFNLKR SDGSWSGYRE VEKLASLSGI
QLRTGCFCNP GACAKYLGLS HLDLRSNFEA GHVCWDDHDI IHEKPTGAVR VSFGYMSTFE
DAKKFIDFVT SSFIALPNWI ESGYQLMQGS ESRLGAASFY LKSITVYPIK SCAGFNVESW
PLSTTAGLLH DREWVLASLS GEILTQKKVP EMCFISTFID LDKGILFVES PRCQVKLPIN
FITDSCNGGS EQIKLNGQRY EVQSYKNEVN IWFSNAIGRP CTLFRCFSSS HNFCLNKIKS
ASMRREVQSV LNFSNEAQFL LISEESVSDL SHRVSTKDVQ KGACGAASQI SPMRFRPNIV
ISGGEPYAED GWKILKIGNK YFTSLGGCNR CQMINIVHDE AGLLQKSNEP LATLASYRRM
KGKIFFGILL KYERSEPVGR DGDLWLQVGQ DVHPNVS
//
