ID A0A1M3EHP2_9CELL Unreviewed; 211 AA.
AC A0A1M3EHP2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=BGO38_07275 {ECO:0000313|EMBL:OJV58007.1};
OS Cellulomonas sp. 73-145.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV58007.1, ECO:0000313|Proteomes:UP000184491};
RN [1] {ECO:0000313|EMBL:OJV58007.1, ECO:0000313|Proteomes:UP000184491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-145 {ECO:0000313|EMBL:OJV58007.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJV58007.1}.
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DR EMBL; MKTI01000009; OJV58007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3EHP2; -.
DR STRING; 1895739.BGO38_07275; -.
DR Proteomes; UP000184491; 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}.
SQ SEQUENCE 211 AA; 20825 MW; ED459D6E90ED07AD CRC64;
MPTVLDQLSA HRLVPVVVID DSAQAGPLAQ ALVDGGLPVA EVTFRTAAAA DAIRAMADRG
DVLVGAGTVL TPAQVDAAVA AGAHYVVSPG TDRAVVERAQ EHGVLALPGA VTATEVQAAL
ALGLTTVKFF PAGTSGGAAA IAALAAPFGG VGFVPTGGVG PKNLGEYLAL PSVKAVGGSW
MVPRDRVAAG DLAGVRDLVA EAVRLASSLR P
//
