ID R5A6N1_9CLOT Unreviewed; 322 AA.
AC R5A6N1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BN452_00687 {ECO:0000313|EMBL:CCX36667.1};
OS Clostridium sp. CAG:1013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262769 {ECO:0000313|EMBL:CCX36667.1, ECO:0000313|Proteomes:UP000018382};
RN [1] {ECO:0000313|EMBL:CCX36667.1, ECO:0000313|Proteomes:UP000018382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1013 {ECO:0000313|Proteomes:UP000018382};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX36667.1}.
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DR EMBL; CAWF010000003; CCX36667.1; -; Genomic_DNA.
DR AlphaFoldDB; R5A6N1; -.
DR Proteomes; UP000018382; 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 InterPro; IPR037523; VOC.
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.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000018382}.
FT DOMAIN 211..320
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 322 AA; 34741 MW; DE66D6D961AA2249 CRC64;
MDKRLELISA VGIVPTIEID DEKKAVPLAK ALVAGGLPIA EVTFRTDAAE ESIHRISQEC
PEVLVGAGTV LTCKQVDMAL EAGSKFIVTP GFHPEVIRYA LSKGALVIPG TSTPGEMEQA
MGLGLNVVKF FPAEQNGGAA KLKALTGPYK TLKWLPTGGI DTAKINEYLS CDQVLACGGS
WMAKQELIKN EDWDGITALC KETVRTMLGF KVVHVGINCK DAAEAEQVAR LFCFLFDVPY
LPNETAIFAG SLVECIKGPY LGAHGHIAIG THNVDRAVYQ LKKRGVIFDE SSRKVDTQGH
TTLIYFKEEI GGFALHLVKS KP
//
