ID D4M8Q8_9BACT Unreviewed; 320 AA.
AC D4M8Q8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=SY1_10350 {ECO:0000313|EMBL:CBL28253.1};
OS Fretibacterium fastidiosum.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=651822 {ECO:0000313|EMBL:CBL28253.1, ECO:0000313|Proteomes:UP000008957};
RN [1] {ECO:0000313|EMBL:CBL28253.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL28253.1,
RC ECO:0000313|Proteomes:UP000008957};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Wade W., Vartoukian S.;
RT "The genome sequence of Synergistetes sp. SGP1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL28253.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL28253.1,
RC ECO:0000313|Proteomes:UP000008957};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929056; CBL28253.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M8Q8; -.
DR KEGG; sbr:SY1_10350; -.
DR PATRIC; fig|651822.3.peg.245; -.
DR HOGENOM; CLU_075245_0_0_0; -.
DR BioCyc; FFAS651822:G13GF-659-MONOMER; -.
DR Proteomes; UP000008957; 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:CBL28253.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008957}.
SQ SEQUENCE 320 AA; 34340 MW; C2B977E39AF03D01 CRC64;
MIDVIKKIRD IGIVPVVKLD SSEQAVPLGK ALIAGGIPIV EVTFRTDAAE ESIKKLVAEL
PEIMVGAGTV TTIDQAKRAW AAGAKFMVSP GFNPNVVRWC IENNIPITPG VNSPSQIEQG
IESGLSVLKF FPAEQSGGVN TLKAFAGPYG SVMYIPTGGV NLKNMCSYLA FKNVLAVGGS
WMVKPDTIAA GKYDEITKLC REAVITGLGF ELRHVGINDP DEDAARRDAA RMEELFSFTS
KPGNSSIFAG VGFEFMKSPY LGKNGHIAIA TYSVDRAVAW LANLGVKTRP DTEKRDSMGS
LTVAYLDEEI GGFAVHLVRR
//
