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MTNC_XANOR
ID   MTNC_XANOR              Reviewed;         232 AA.
AC   Q5H0Y0; Q6GYR5;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_01681};
DE            EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_01681};
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_01681};
GN   Name=mtnC {ECO:0000255|HAMAP-Rule:MF_01681}; OrderedLocusNames=XOO2137;
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhang Y., Wang J.;
RT   "Overexpression of the enolase-phosphatase-like gene in vivo reduces the
RT   fitness of Xanthomonas oryzae pv. oryzae in rice cultivars.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85;
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA   Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA   Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA   Go S.-J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-
CC       diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC       intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-
CC       MTPenyl-1-P), which is then dephosphorylated to form the acireductone
CC       1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
CC       {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-
CC         dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC         Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01681};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01681};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01681};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC       step 3/6. {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC       step 4/6. {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC       family. {ECO:0000255|HAMAP-Rule:MF_01681}.
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DR   EMBL; AY588249; AAT48366.2; -; Genomic_DNA.
DR   EMBL; AE013598; AAW75391.1; -; Genomic_DNA.
DR   RefSeq; WP_011258836.1; NC_006834.1.
DR   AlphaFoldDB; Q5H0Y0; -.
DR   SMR; Q5H0Y0; -.
DR   STRING; 291331.XOO2137; -.
DR   EnsemblBacteria; AAW75391; AAW75391; XOO2137.
DR   KEGG; xoo:XOO2137; -.
DR   HOGENOM; CLU_023273_0_0_6; -.
DR   OMA; QLKGHVY; -.
DR   BRENDA; 3.1.3.77; 9368.
DR   BRENDA; 4.2.1.11; 6717.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000006735; Chromosome.
DR   GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   CDD; cd01629; HAD_EP; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01681; Salvage_MtnC; 1.
DR   InterPro; IPR023943; Enolase-ppase_E1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDF00044; enolase-phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Methionine biosynthesis; Reference proteome.
FT   CHAIN           1..232
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000357432"
FT   CONFLICT        198
FT                   /note="I -> M (in Ref. 1; AAT48366)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="S -> N (in Ref. 1; AAT48366)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   232 AA;  25931 MW;  89F69B08F5DDD0E8 CRC64;
     MTRPQAILTD IEGTTSSISF VKDVLFPYAR RAMPAYVREH GNHPQVRHWL NQVADEIGED
     VPDDVLITTL QTWIDEDRKH TALKALQGLI WGDGYKIADF TAHMYADAAL QLQAWHAAGI
     PLYVYSSGSV PAQKLFFAHS DAGDLSGLVS DWFDTEVGSK REAASYRRIA ERIGVPASEI
     LFLSDVIEEL DAAKRTGIRT ALLERREDYP TPRSADDVGS HQRVESFSQL VF
 
 
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