ID   ALKD_PSEA6              Reviewed;         215 AA.
AC   Q15X88;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase {ECO:0000305};
DE            EC=4.1.2.14 {ECO:0000269|Ref.2};
DE   AltName: Full=2-keto-3-deoxy-6-phospho-D-gluconate aldolase {ECO:0000303|Ref.2};
DE   AltName: Full=KDPG aldolase {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Patl_0974 {ECO:0000312|EMBL:ABG39500.1};
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=3042615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA   Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=T6c / ATCC BAA-1087;
RX   DOI=10.1007/s12257-014-0622-3;
RA   Lee S.B., Cho S.J., Kim J.A., Lee S.Y., Kim S.M., Lim H.S.;
RT   "Metabolic pathway of 3,6-anhydro-L-galactose in agar-degrading
RT   microorganisms.";
RL   Biotechnol. Bioprocess Eng. 19:866-878(2014).
CC   -!- FUNCTION: Involved in the degradation of 3,6-anhydro-L-galactose, which
CC       is the major monomeric sugar of red macroalgae. Catalyzes the sixth
CC       step of the pathway, the cleavage of 2-dehydro-3-deoxy-6-phospho-D-
CC       gluconate (KDPG) to glyceraldehyde 3-phosphate and pyruvate.
CC       {ECO:0000269|Ref.2}.
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:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR   EMBL; CP000388; ABG39500.1; -; Genomic_DNA.
DR   RefSeq; WP_006990598.1; NC_008228.1.
DR   AlphaFoldDB; Q15X88; -.
DR   SMR; Q15X88; -.
DR   STRING; 342610.Patl_0974; -.
DR   KEGG; pat:Patl_0974; -.
DR   eggNOG; COG0800; Bacteria.
DR   HOGENOM; CLU_077795_1_1_6; -.
DR   OrthoDB; 9805177at2; -.
DR   BioCyc; MetaCyc:MONOMER-19469; -.
DR   Proteomes; UP000001981; Chromosome.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Lyase.
FT   CHAIN           1..215
FT                   /note="2-dehydro-3-deoxy-phosphogluconate aldolase"
FT                   /id="PRO_0000449957"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   ACT_SITE        134
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A955"
SQ   SEQUENCE   215 AA;  22132 MW;  4C80E2F6A23BA982 CRC64;
     MTKNWKVSSQ DVFSQGPVVP VLVIKDVKHA VPLAKALIAG GIRVLEVTLR TEAALDVIKA
     IATEVPDAII GAGTVTNAKQ LAEVEAAGAM FAISPGMTSD LLDAGNKGGI ALIPGISSIS
     ELMRGIDFGY THFKFFPAEA SGGVKAIKAI GGPFPDIAFC PTGGISPTNY LEYLSLPNVR
     CAGGSWLAPD DAVEAGDWDR ITELAKQAVA GAAGI
//