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Database: UniProt
Entry: A0A0J5GJ11_9NEIS
LinkDB: A0A0J5GJ11_9NEIS
Original site: A0A0J5GJ11_9NEIS 
ID   A0A0J5GJ11_9NEIS        Unreviewed;       208 AA.
AC   A0A0J5GJ11;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=ACG97_03055 {ECO:0000313|EMBL:KMJ54347.1};
OS   Vogesella sp. EB.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ54347.1, ECO:0000313|Proteomes:UP000054352};
RN   [1] {ECO:0000313|EMBL:KMJ54347.1, ECO:0000313|Proteomes:UP000054352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB {ECO:0000313|EMBL:KMJ54347.1,
RC   ECO:0000313|Proteomes:UP000054352};
RA   Arrua Day P., Revale S., Alvarez H.M.;
RT   "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT   Vogesella sp. strain EB.";
RL   Submitted (JUN-2015) 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:KMJ54347.1}.
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DR   EMBL; LFDT01000003; KMJ54347.1; -; Genomic_DNA.
DR   RefSeq; WP_047965859.1; NZ_LFDT01000003.1.
DR   AlphaFoldDB; A0A0J5GJ11; -.
DR   STRING; 1526735.ACG97_03055; -.
DR   PATRIC; fig|1526735.3.peg.652; -.
DR   OrthoDB; 9805177at2; -.
DR   Proteomes; UP000054352; 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, ECO:0000313|EMBL:KMJ54347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054352}.
SQ   SEQUENCE   208 AA;  21436 MW;  F8FFFA26F6579580 CRC64;
     MDALTLLRQG PVMPVIVVND AAVAVDLARA LVAGGIRTLE ITLRTKAALA AMRRIRDEVP
     DAIVGAGTVR TRAHLEAALD AGAQFGISPG LTPELAAAAR AANVPFIPGV ATPSEAMHAQ
     DEGFNILKLF PAEAVGGIKL LKALAGPLPE LRFCPTGGID INSAPNYLAL PNVLCVGGSW
     LTPDDAIAAQ DWARITALAQ QASALAVR
//
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