ID A0A0Q0AV52_PSESX Unreviewed; 224 AA.
AC A0A0Q0AV52;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase {ECO:0000256|ARBA:ARBA00013063};
DE EC=4.1.2.14 {ECO:0000256|ARBA:ARBA00013063};
GN ORFNames=ALO94_00061 {ECO:0000313|EMBL:KPY66679.1}, ALP50_03891
GN {ECO:0000313|EMBL:RMT32736.1};
OS Pseudomonas syringae pv. spinaceae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=264459 {ECO:0000313|EMBL:KPY66679.1, ECO:0000313|Proteomes:UP000050384};
RN [1] {ECO:0000313|EMBL:KPY66679.1, ECO:0000313|Proteomes:UP000050384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP16929 {ECO:0000313|EMBL:KPY66679.1,
RC ECO:0000313|Proteomes:UP000050384};
RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT "Genome announcement of multiple Pseudomonas syringae strains.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RMT32736.1, ECO:0000313|Proteomes:UP000280047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 16928 {ECO:0000313|EMBL:RMT32736.1,
RC ECO:0000313|Proteomes:UP000280047};
RA Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.;
RT "Recombination of ecologically and evolutionarily significant loci
RT maintains genetic cohesion in the Pseudomonas syringae species complex.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPY66679.1}.
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DR EMBL; LJRI01001271; KPY66679.1; -; Genomic_DNA.
DR EMBL; RBTF01000182; RMT32736.1; -; Genomic_DNA.
DR RefSeq; WP_005764046.1; NZ_RBTF01000182.1.
DR AlphaFoldDB; A0A0Q0AV52; -.
DR GeneID; 1182938; -.
DR PATRIC; fig|264459.3.peg.104; -.
DR Proteomes; UP000050384; Unassembled WGS sequence.
DR Proteomes; UP000280047; Unassembled WGS sequence.
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 InterPro; IPR031338; KDPG/KHG_AS_2.
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.
DR PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
SQ SEQUENCE 224 AA; 23877 MW; F1FCFF7469C34FE9 CRC64;
MTQNENNQPL TSMANKIARI DELCAKAKIL PVITIARDQD VLPLADALAA GGMTALEITL
RSAFGLSAIR ILREQRPELC TGAGTILDRK MLADAEAAGS QFIVTPGSTQ ELLQAALDSP
LPLLPGVSSA SEIMIGYALG YRRFKLFPAE ISGGVAAIKA LGGPFNEVRF CPTGGVNEQN
LKNYMALPNV MCVGGTWMID NAWVKNGDWG RIQEATAQAL ALFD
//
