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Database: UniProt
Entry: A4YP52_BRASO
LinkDB: A4YP52_BRASO
Original site: A4YP52_BRASO 
ID   A4YP52_BRASO            Unreviewed;       214 AA.
AC   A4YP52;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=eda {ECO:0000313|EMBL:CAL75678.1};
GN   OrderedLocusNames=BRADO1806 {ECO:0000313|EMBL:CAL75678.1};
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL75678.1, ECO:0000313|Proteomes:UP000001994};
RN   [1] {ECO:0000313|EMBL:CAL75678.1, ECO:0000313|Proteomes:UP000001994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CU234118; CAL75678.1; -; Genomic_DNA.
DR   RefSeq; WP_011924906.1; NC_009445.1.
DR   AlphaFoldDB; A4YP52; -.
DR   STRING; 114615.BRADO1806; -.
DR   KEGG; bra:BRADO1806; -.
DR   eggNOG; COG0800; Bacteria.
DR   HOGENOM; CLU_077795_1_1_5; -.
DR   OrthoDB; 9805177at2; -.
DR   Proteomes; UP000001994; 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   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:CAL75678.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001994}.
SQ   SEQUENCE   214 AA;  21888 MW;  C83919107E9A1BEA CRC64;
     MMSNPDNRAK LDAVFALAPV IPVITIEDAA QAVPLARALV AGGLRVIEIT LRTQAGFDAA
     RAIIGEVPEA KVGIGTVLTP ADYERAAKLG AAFAISPGMS IELLDAASSG DLPFAPGIQT
     PSDLIACVTR GYELVKFFPA VPAGGLAALD ALAGPFPSVR FCPTGGINAA NAAQWLAHKK
     VVAIGGSWVA PAADIKAGAW VAIQQRAREA TALR
//
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