ALKH_ZYMMO
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 03-AUG-2022, entry version 117.
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; Proteobacteria; 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 EnsemblBacteria; AAV89621; AAV89621; ZMO0997.
DR GeneID; 58026787; -.
DR KEGG; zmo:ZMO0997; -.
DR eggNOG; COG0800; Bacteria.
DR HOGENOM; CLU_077795_1_1_5; -.
DR OMA; FFPAEYC; -.
DR OrthoDB; 1497385at2; -.
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; -; 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 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
