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Database: UniProt
Entry: N9UXY5_9SPHN
LinkDB: N9UXY5_9SPHN
Original site: N9UXY5_9SPHN 
ID   N9UXY5_9SPHN            Unreviewed;       206 AA.
AC   N9UXY5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=EBMC1_00500 {ECO:0000313|EMBL:ENY83275.1};
OS   Sphingopyxis sp. MC1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY83275.1, ECO:0000313|Proteomes:UP000013072};
RN   [1] {ECO:0000313|EMBL:ENY83275.1, ECO:0000313|Proteomes:UP000013072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|EMBL:ENY83275.1,
RC   ECO:0000313|Proteomes:UP000013072};
RA   Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT   "Differential expression analysis of membrane associated proteins from
RT   triclosan-degrading sphingopyxis.";
RL   Submitted (FEB-2013) 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:ENY83275.1}.
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DR   EMBL; AOUN01000001; ENY83275.1; -; Genomic_DNA.
DR   RefSeq; WP_003038854.1; NZ_AOUN01000001.1.
DR   AlphaFoldDB; N9UXY5; -.
DR   PATRIC; fig|1174684.3.peg.103; -.
DR   eggNOG; COG0800; Bacteria.
DR   Proteomes; UP000013072; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013072}.
SQ   SEQUENCE   206 AA;  20498 MW;  7D4E66EB74E322AE CRC64;
     MTDKSIDQIM ALAPVIPVIV IDCVEDAVPM AEALVAGGLP VLEVTLRTPA ALAAIAAMKA
     VPGAVVGAGT VLDPAMLAGA IHAGAEFIVS PGLTDNLGEA AVASGIPFLP GTANAGDIMR
     GMDLGLSHFK FFPAATSGGI PALKALAGPF GQARFCPTGG ITAATAPEWL ALDPVLCVGG
     SWVVPAGPLD PARIETLARE ASAFKP
//
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