ID B3PCY9_CELJU Unreviewed; 210 AA.
AC B3PCY9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase {ECO:0000256|ARBA:ARBA00013063};
DE EC=4.1.2.14 {ECO:0000256|ARBA:ARBA00013063};
GN Name=kdgA {ECO:0000313|EMBL:ACE84201.1};
GN OrderedLocusNames=CJA_1352 {ECO:0000313|EMBL:ACE84201.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84201.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE84201.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84201.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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 Evidence={ECO:0000256|ARBA:ARBA00000654};
CC -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family.
CC {ECO:0000256|ARBA:ARBA00006906}.
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DR EMBL; CP000934; ACE84201.1; -; Genomic_DNA.
DR RefSeq; WP_012486988.1; NC_010995.1.
DR AlphaFoldDB; B3PCY9; -.
DR STRING; 498211.CJA_1352; -.
DR KEGG; cja:CJA_1352; -.
DR eggNOG; COG0800; Bacteria.
DR HOGENOM; CLU_077795_1_1_6; -.
DR OrthoDB; 9805177at2; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR CDD; cd00452; KDPG_aldolase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR000887; Aldlse_KDPG_KHG.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR031337; KDPG/KHG_AS_1.
DR NCBIfam; TIGR01182; eda; 1.
DR PANTHER; PTHR30246; 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE; 1.
DR PANTHER; PTHR30246:SF2; KHG_KDPG ALDOLASE; 1.
DR Pfam; PF01081; Aldolase; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ACE84201.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036}.
SQ SEQUENCE 210 AA; 21789 MW; CF0D8F915358FD6B CRC64;
MALTIDQILK VAPVVPVMVV ERIEDAVPLA TALYNGGLKV LEITLRTPCA LDAISAMVEA
LPDDAVIGAG TIITPKDLDA AVKAGSTFMV SPGTTPALIE AAKACPVPLL AGVATPTEAM
HLLVEGFTHQ KFFPAEAAGG VPMLKSIAGP LPQITFCPTG GIDLAKAPSY LALPNVACVG
GTWMAPKELM KAGRWEEIER LAREAASLPR
//
