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ALKH_TREPA
ID   ALKH_TREPA              Reviewed;         210 AA.
AC   O83578;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative KHG/KDPG aldolase;
DE   Includes:
DE     RecName: Full=4-hydroxy-2-oxoglutarate aldolase;
DE              EC=4.1.3.16;
DE     AltName: Full=2-keto-4-hydroxyglutarate aldolase;
DE              Short=KHG-aldolase;
DE   Includes:
DE     RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase;
DE              EC=4.1.2.14;
DE     AltName: Full=2-keto-3-deoxy-6-phosphogluconate aldolase;
DE              Short=KDPG-aldolase;
DE     AltName: Full=Phospho-2-dehydro-3-deoxygluconate aldolase;
DE     AltName: Full=Phospho-2-keto-3-deoxygluconate aldolase;
GN   Name=eda; OrderedLocusNames=TP_0568;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:71685; EC=4.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC         Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:62213; EC=4.1.3.16;
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   -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC       degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC       3-deoxy-D-gluconate: step 2/2.
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate and dicarboxylate
CC       metabolism.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR   EMBL; AE000520; AAC65542.1; -; Genomic_DNA.
DR   PIR; F71308; F71308.
DR   RefSeq; WP_010882015.1; NC_021490.2.
DR   AlphaFoldDB; O83578; -.
DR   SMR; O83578; -.
DR   STRING; 243276.TPANIC_0568; -.
DR   EnsemblBacteria; AAC65542; AAC65542; TP_0568.
DR   GeneID; 57879092; -.
DR   KEGG; tpa:TP_0568; -.
DR   eggNOG; COG0800; Bacteria.
DR   HOGENOM; CLU_077795_1_1_12; -.
DR   OMA; FFPAEYC; -.
DR   OrthoDB; 1175355at2; -.
DR   UniPathway; UPA00227; -.
DR   UniPathway; UPA00856; UER00829.
DR   Proteomes; UP000000811; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR   GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00452; KDPG_aldolase; 1.
DR   Gene3D; 3.20.20.70; -; 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   PANTHER; PTHR30246; PTHR30246; 1.
DR   Pfam; PF01081; Aldolase; 1.
DR   TIGRFAMs; TIGR01182; eda; 1.
DR   PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1.
DR   PROSITE; PS00160; ALDOLASE_KDPG_KHG_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Multifunctional enzyme; Reference proteome; Schiff base.
FT   CHAIN           1..210
FT                   /note="Putative KHG/KDPG aldolase"
FT                   /id="PRO_0000201043"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   ACT_SITE        129
FT                   /note="Schiff-base intermediate with KHG or pyruvate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
SQ   SEQUENCE   210 AA;  22074 MW;  7DC3408B01C244E7 CRC64;
     MITIFEALER VRVIPVVTLE RVEDAVPLAR ALITGGIRCM EVTFRTLVAA EAIAAIRQEC
     ADVLLGAGTV LTVEQAQQAQ AAGAQFVVSP GFNPRVVAHC LGHGVPIIPG IASATEIERA
     LEFGISVVKF FPAELLGGTA MMSALARPYT AVRFVPTGGI HLNNLAEYVA HPRVLACGGS
     WMVPAQSIAA GDFSQVTALS QQTLQIVGVM
 
 
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