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ALKH_BACSU
ID   ALKH_BACSU              Reviewed;         196 AA.
AC   P50846;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=KHG/KDPG aldolase;
DE   Includes:
DE     RecName: Full=4-hydroxy-2-oxoglutarate aldolase;
DE              EC=4.1.3.16;
DE     AltName: Full=2-keto-4-hydroxyglutarate aldolase;
DE              Short=KHG-aldolase;
DE   Includes:
DE     RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase;
DE              EC=4.1.2.14;
DE     AltName: Full=2-keto-3-deoxy-6-phosphogluconate aldolase;
DE              Short=KDPG-aldolase;
DE     AltName: Full=Phospho-2-dehydro-3-deoxygluconate aldolase;
DE     AltName: Full=Phospho-2-keto-3-deoxygluconate aldolase;
GN   Name=kdgA; OrderedLocusNames=BSU22100;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA   Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA   Serror P.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   serA and kdg loci cloned in a yeast artificial chromosome.";
RL   Microbiology 142:2005-2016(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=9846747; DOI=10.1099/00221287-144-11-3111;
RA   Pujic P., Dervyn R., Sorokin A., Ehrlich S.D.;
RT   "The kdgRKAT operon of Bacillus subtilis: detection of the transcript and
RT   regulation by the kdgR and ccpA genes.";
RL   Microbiology 144:3111-3118(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:71685; EC=4.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:62213; EC=4.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-
CC         phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.14;
CC   -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC       degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC       3-deoxy-D-gluconate: step 2/2.
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate and dicarboxylate
CC       metabolism.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Induced by galacturonate and negatively regulated by the
CC       KdgR repressor. Is subject to catabolite repression by glucose
CC       involving the ccpA gene. {ECO:0000269|PubMed:9846747}.
CC   -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR   EMBL; L47838; AAB38480.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14127.1; -; Genomic_DNA.
DR   PIR; H69647; H69647.
DR   RefSeq; NP_390092.1; NC_000964.3.
DR   RefSeq; WP_003230732.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P50846; -.
DR   SMR; P50846; -.
DR   STRING; 224308.BSU22100; -.
DR   jPOST; P50846; -.
DR   PaxDb; P50846; -.
DR   PRIDE; P50846; -.
DR   EnsemblBacteria; CAB14127; CAB14127; BSU_22100.
DR   GeneID; 939066; -.
DR   KEGG; bsu:BSU22100; -.
DR   PATRIC; fig|224308.179.peg.2414; -.
DR   eggNOG; COG0800; Bacteria.
DR   InParanoid; P50846; -.
DR   OMA; HGPIPEV; -.
DR   PhylomeDB; P50846; -.
DR   BioCyc; BSUB:BSU22100-MON; -.
DR   UniPathway; UPA00227; -.
DR   UniPathway; UPA00856; UER00829.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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   TIGRFAMs; TIGR01182; eda; 1.
DR   PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Multifunctional enzyme; Reference proteome; Schiff base.
FT   CHAIN           1..196
FT                   /note="KHG/KDPG aldolase"
FT                   /id="PRO_0000201036"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        130
FT                   /note="Schiff-base intermediate with KHG or pyruvate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   196 AA;  20865 MW;  EB0B597FD1102CC4 CRC64;
     MESKVVENRL KEAKLIAVIR SKDKQEACQQ IESLLDKGIR AVEVTYTTPG ASDIIESFRN
     REDILIGAGT VISAQQAGEA AKAGAQFIVS PGFSADLAEH LSFVKTHYIP GVLTPSEIME
     ALTFGFTTLK LFPSGVFGIP FMKNLAGPFP QVTFIPTGGI HPSEVPDWLR AGAGAVGVGS
     QLGSCSKEDL QAVFQV
 
 
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