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Database: UniProt
Entry: A5PED0_9SPHN
LinkDB: A5PED0_9SPHN
Original site: A5PED0_9SPHN 
ID   A5PED0_9SPHN            Unreviewed;       204 AA.
AC   A5PED0;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=ED21_22303 {ECO:0000313|EMBL:EDL47888.1};
OS   Erythrobacter sp. SD-21.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL47888.1, ECO:0000313|Proteomes:UP000005498};
RN   [1] {ECO:0000313|EMBL:EDL47888.1, ECO:0000313|Proteomes:UP000005498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD-21 {ECO:0000313|EMBL:EDL47888.1,
RC   ECO:0000313|Proteomes:UP000005498};
RA   Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDL47888.1}.
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DR   EMBL; ABCG01000010; EDL47888.1; -; Genomic_DNA.
DR   RefSeq; WP_006834508.1; NZ_ABCG01000010.1.
DR   AlphaFoldDB; A5PED0; -.
DR   STRING; 161528.ED21_22303; -.
DR   eggNOG; COG0800; Bacteria.
DR   OrthoDB; 9805177at2; -.
DR   Proteomes; UP000005498; 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:SF1; 2-DEHYDRO-3-DEOXY-6-PHOSPHOGALACTONATE ALDOLASE; 1.
DR   PANTHER; PTHR30246; 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005498}.
SQ   SEQUENCE   204 AA;  20883 MW;  A0D632BEDE1B4833 CRC64;
     MTHIADIMQT APVIPVIVVD EMEHAVPLAR ALVAGGLRVL EVTLRTPAAL DAIRAMKKVD
     GAIVGAGTVT NQEELAAAID AGSEFIVSPG LTEPLGKAAI REGIPFLPGI ANAGDIMRGL
     DLGLTHFKFF PAMAAGGLPA LKALAAPFGQ CRFCPTGGIT LENAPDWLGF DPVLCVGGSW
     VAPRSAVDEA AVEKVAREAA ALGG
//
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