ID   ALKH_ZYMMO              Reviewed;         208 AA.
AC   Q00384; Q5NNT9;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=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; Synonyms=kdgA; OrderedLocusNames=ZMO0997;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=1809834; DOI=10.1111/j.1365-2958.1991.tb01850.x;
RA   Conway T., Fliege R., Jones-Kilpatrick D., Liu J., Barnell W.O., Egan S.E.;
RT   "Cloning, characterization and expression of the Zymononas mobilis eda gene
RT   that encodes 2-keto-3-deoxy-6-phosphogluconate aldolase of the Entner-
RT   Doudoroff pathway.";
RL   Mol. Microbiol. 5:2901-2911(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the KHG/KDPG aldolase family. {ECO:0000305}.
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DR   EMBL; X58364; CAA41258.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89621.1; -; Genomic_DNA.
DR   RefSeq; WP_011240846.1; NZ_CP035711.1.
DR   PDB; 5XSE; X-ray; 1.80 A; A/B/C=1-208.
DR   PDB; 5XSF; X-ray; 1.96 A; A=1-208.
DR   PDBsum; 5XSE; -.
DR   PDBsum; 5XSF; -.
DR   AlphaFoldDB; Q00384; -.
DR   SMR; Q00384; -.
DR   STRING; 264203.ZMO0997; -.
DR   GeneID; 79903862; -.
DR   KEGG; zmo:ZMO0997; -.
DR   eggNOG; COG0800; Bacteria.
DR   HOGENOM; CLU_077795_1_1_5; -.
DR   BRENDA; 4.1.2.14; 14380.
DR   UniPathway; UPA00227; -.
DR   UniPathway; UPA00856; UER00829.
DR   Proteomes; UP000001173; 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; 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:SF1; 2-DEHYDRO-3-DEOXY-6-PHOSPHOGALACTONATE ALDOLASE; 1.
DR   PANTHER; PTHR30246; 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lyase; Multifunctional enzyme; Reference proteome;
KW   Schiff base.
FT   CHAIN           1..208
FT                   /note="KHG/KDPG aldolase"
FT                   /id="PRO_0000201044"
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        128
FT                   /note="Schiff-base intermediate with KHG or pyruvate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10118"
FT   CONFLICT        1..4
FT                   /note="MRDI -> M (in Ref. 1; CAA41258)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..9
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          12..17
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           25..34
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           49..56
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           72..80
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           93..101
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           113..121
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           164..168
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   STRAND          176..179
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   HELIX           189..200
FT                   /evidence="ECO:0007829|PDB:5XSE"
FT   TURN            205..207
FT                   /evidence="ECO:0007829|PDB:5XSE"
SQ   SEQUENCE   208 AA;  21505 MW;  1685B45A7DFB57B4 CRC64;
     MRDIDSVMRL APVMPVLVIE DIADAKPIAE ALVAGGLNVL EVTLRTPCAL EAIKIMKEVP
     GAVVGAGTVL NAKMLDQAQE AGCEFFVSPG LTADLGKHAV AQKAALLPGV ANAADVMLGL
     DLGLDRFKFF PAENIGGLPA LKSMASVFRQ VRFCPTGGIT PTSAPKYLEN PSILCVGGSW
     VVPAGKPDVA KITALAKEAS AFKRAAVA
//