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DGOA_RHIME
ID   DGOA_RHIME              Reviewed;         212 AA.
AC   Q92RN8;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Probable 2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
DE            EC=4.1.2.21;
DE   AltName: Full=2-oxo-3-deoxygalactonate 6-phosphate aldolase;
DE   AltName: Full=6-phospho-2-dehydro-3-deoxygalactonate aldolase;
DE   AltName: Full=6-phospho-2-keto-3-deoxygalactonate aldolase;
DE            Short=KDPGal;
GN   Name=dgoA; OrderedLocusNames=R00824; ORFNames=SMc00882;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=1021;
RX   PubMed=22797764; DOI=10.1128/jb.00982-12;
RA   Geddes B.A., Oresnik I.J.;
RT   "Inability to catabolize galactose leads to increased ability to compete
RT   for nodule occupancy in Sinorhizobium meliloti.";
RL   J. Bacteriol. 194:5044-5053(2012).
CC   -!- FUNCTION: Involved in the degradation of galactose via the DeLey-
CC       Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol
CC       cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate
CC       and D-glyceraldehyde-3-phosphate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde
CC         3-phosphate + pyruvate; Xref=Rhea:RHEA:24464, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:58298, ChEBI:CHEBI:59776; EC=4.1.2.21;
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-galactonate degradation; D-
CC       glyceraldehyde 3-phosphate and pyruvate from D-galactonate: step 3/3.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on galactose
CC       as sole carbon source. {ECO:0000269|PubMed:22797764}.
CC   -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR   EMBL; AL591688; CAC45396.1; -; Genomic_DNA.
DR   RefSeq; NP_384930.1; NC_003047.1.
DR   RefSeq; WP_010968849.1; NC_003047.1.
DR   AlphaFoldDB; Q92RN8; -.
DR   SMR; Q92RN8; -.
DR   STRING; 266834.SMc00882; -.
DR   EnsemblBacteria; CAC45396; CAC45396; SMc00882.
DR   GeneID; 61602290; -.
DR   KEGG; sme:SMc00882; -.
DR   PATRIC; fig|266834.11.peg.2214; -.
DR   eggNOG; COG0800; Bacteria.
DR   HOGENOM; CLU_077795_2_1_5; -.
DR   OMA; HGPIPEV; -.
DR   UniPathway; UPA00081; UER00520.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0008674; F:2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034194; P:D-galactonate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00452; KDPG_aldolase; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR000887; Aldlse_KDPG_KHG.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR031338; KDPG/KHG_AS_2.
DR   PANTHER; PTHR30246; PTHR30246; 1.
DR   Pfam; PF01081; Aldolase; 1.
DR   PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..212
FT                   /note="Probable 2-dehydro-3-deoxy-6-phosphogalactonate
FT                   aldolase"
FT                   /id="PRO_0000428930"
FT   ACT_SITE        41
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        130
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            18
FT                   /note="Orients the nucleophilic substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            158
FT                   /note="Plays a major role in determining the
FT                   stereoselectivity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  21588 MW;  EC344AEEE5300551 CRC64;
     MDRIPLPPME RPLIAILRGL KPEEAEGVVG ALIETGFTAI EIPLNSPDPF RSIETAVKMA
     PAGCLIGAGT VLTTAQVERL ADVGGRLMVS PNVEPAVIRL AATKGMVTMP GVFTPTEALA
     AAAAGASGLK FFPASVLGPS GITAIRAVLP GDLEIAAVGG VSEVNFADYA AIGIRSFGLG
     SSLYKPGMSA GDVRQRAIAT LAAYDAVYGG QQ
 
 
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