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KDGD_AZOVD
ID   KDGD_AZOVD              Reviewed;         303 AA.
AC   C1DJJ0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable 5-dehydro-4-deoxyglucarate dehydratase {ECO:0000255|HAMAP-Rule:MF_00694};
DE            EC=4.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00694};
DE   AltName: Full=5-keto-4-deoxy-glucarate dehydratase {ECO:0000255|HAMAP-Rule:MF_00694};
DE            Short=KDGDH {ECO:0000255|HAMAP-Rule:MF_00694};
GN   OrderedLocusNames=Avin_05220;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-dehydro-4-deoxy-D-glucarate + H(+) = 2,5-dioxopentanoate +
CC         CO2 + H2O; Xref=Rhea:RHEA:24608, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:42819,
CC         ChEBI:CHEBI:58136; EC=4.2.1.41; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00694};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-glucarate degradation; 2,5-
CC       dioxopentanoate from D-glucarate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00694}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00694}.
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DR   EMBL; CP001157; ACO76775.1; -; Genomic_DNA.
DR   RefSeq; WP_012699203.1; NC_012560.1.
DR   AlphaFoldDB; C1DJJ0; -.
DR   SMR; C1DJJ0; -.
DR   STRING; 322710.Avin_05220; -.
DR   EnsemblBacteria; ACO76775; ACO76775; Avin_05220.
DR   KEGG; avn:Avin_05220; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_5_2_6; -.
DR   OMA; EFHALTP; -.
DR   OrthoDB; 1438588at2; -.
DR   UniPathway; UPA00564; UER00628.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0047448; F:5-dehydro-4-deoxyglucarate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042838; P:D-glucarate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00951; KDGDH; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00694; KDGDH; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR017655; Dehydro-deoxyglucarate_dehyd.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   SMART; SM01130; DHDPS; 1.
DR   TIGRFAMs; TIGR03249; KdgD; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..303
FT                   /note="Probable 5-dehydro-4-deoxyglucarate dehydratase"
FT                   /id="PRO_1000212623"
SQ   SEQUENCE   303 AA;  32652 MW;  7835093016D034DB CRC64;
     MTPQELKSIL SSGLLSFPVT DFDAAGDFDA ESYARRLEWL APYGASALFA AGGTGEFFSL
     GLDEYPRIIK TAVDTCAGSV PILAGVGGPT RQAIHMAQEA ERLGAKGLLL LPHYLTEASQ
     EGVAAHVEAV CRAVKIGVVV YNRNVCRLTP ALLEQLAERC PNLVGYKDGL GEIELMVSVR
     HRLGERFAYL GGLPTAEVYA AAYKALGVPV YSSAVFNFIP RTAMEFYKAV AADDQVTVGR
     LIDDFFLPLL EIRNRRAGYA VSIVKAGVRV IGHDAGPVRA PLTDLLPDEY ERLAALIRKL
     GPQ
 
 
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