HPCG_ECOLX
ID HPCG_ECOLX Reviewed; 267 AA.
AC P42270;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=2-oxo-hept-4-ene-1,7-dioate hydratase {ECO:0000303|Ref.3};
DE Short=OHED hydratase {ECO:0000303|Ref.3};
DE EC=4.2.1.163 {ECO:0000269|PubMed:17559873, ECO:0000269|Ref.3};
GN Name=hpcG {ECO:0000303|Ref.3};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C;
RX PubMed=7737515; DOI=10.1016/0378-1119(95)00082-h;
RA Roper D.I., Stringfellow J.M., Cooper R.A.;
RT "Sequence of the hpcC and hpcG genes of the meta-fission homoprotocatechuic
RT acid pathway of Escherichia coli C: nearly 40% amino-acid identity with the
RT analogous enzymes of the catechol pathway.";
RL Gene 156:47-51(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C {ECO:0000312|EMBL:AAB91474.1};
RA Burks E.A., Whitman C.P.;
RT "OHED hydratase.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ENZYME KINETICS, AND REACTION MECHANISM.
RC STRAIN=C;
RX DOI=10.1021/ja9808402;
RA Burks E.A., Johnson W.H. Jr., Whitman C.P.;
RT "Stereochemical and isotopic labeling studies of 2-oxo-hept-4-ene-1,7-
RT dioate hydratase: evidence for an enzyme-catalyzed ketonization step in the
RT hydration reaction.";
RL J. Am. Chem. Soc. 120:7665-7675(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP MAGNESIUM AND OXALATE, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND REACTION
RP MECHANISM.
RC STRAIN=C;
RX PubMed=17559873; DOI=10.1016/j.jmb.2007.05.006;
RA Izumi A., Rea D., Adachi T., Unzai S., Park S.Y., Roper D.I., Tame J.R.;
RT "Structure and mechanism of HpcG, a hydratase in the homoprotocatechuate
RT degradation pathway of Escherichia coli.";
RL J. Mol. Biol. 370:899-911(2007).
CC -!- FUNCTION: Transforms 2-oxo-hept-4-ene-1,7-dioate (OHED) into 4-hydroxy-
CC 2-oxoheptanedioate, a step in the 4-hydroxyphenylacetic acid (4-HPA)
CC degradation pathway. {ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z)-2-oxohept-4-enedioate + H2O = (4S)-4-hydroxy-2-
CC oxoheptanedioate; Xref=Rhea:RHEA:42072, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:87507, ChEBI:CHEBI:87522; EC=4.2.1.163;
CC Evidence={ECO:0000269|PubMed:17559873, ECO:0000269|Ref.3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17559873};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17559873};
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 6/7.
CC -!- SUBUNIT: Homodecamer. {ECO:0000269|PubMed:17559873}.
CC -!- SIMILARITY: Belongs to the hydratase/decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X81446; CAA57202.1; -; Genomic_DNA.
DR EMBL; AF036583; AAB91474.1; -; Genomic_DNA.
DR PIR; I41083; I41083.
DR RefSeq; WP_000459750.1; NZ_WVWF01000016.1.
DR PDB; 2EB4; X-ray; 1.60 A; A/B/C/D/E=1-267.
DR PDB; 2EB5; X-ray; 1.70 A; A/B/C/D/E=1-267.
DR PDB; 2EB6; X-ray; 1.69 A; A/B/C/D/E=1-267.
DR PDBsum; 2EB4; -.
DR PDBsum; 2EB5; -.
DR PDBsum; 2EB6; -.
DR AlphaFoldDB; P42270; -.
DR SMR; P42270; -.
DR STRING; 585034.ECIAI1_4571; -.
DR GeneID; 66671765; -.
DR eggNOG; COG3971; Bacteria.
DR OMA; IQRAWVA; -.
DR OrthoDB; 1314120at2; -.
DR BRENDA; 4.2.1.163; 2026.
DR UniPathway; UPA00208; UER00421.
DR GO; GO:0018817; F:2-oxo-hept-3-ene-1,7-dioate hydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR InterPro; IPR012690; HpcG.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
DR TIGRFAMs; TIGR02312; HpaH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Lyase; Magnesium;
KW Metal-binding.
FT CHAIN 1..267
FT /note="2-oxo-hept-4-ene-1,7-dioate hydratase"
FT /id="PRO_0000084042"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17559873,
FT ECO:0007744|PDB:2EB5, ECO:0007744|PDB:2EB6"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17559873,
FT ECO:0007744|PDB:2EB5, ECO:0007744|PDB:2EB6"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17559873,
FT ECO:0007744|PDB:2EB5, ECO:0007744|PDB:2EB6"
FT CONFLICT 85..98
FT /note="DDMFFHDGSDIPTD -> HDNVLPRWQRY (in Ref. 1; CAA57202)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> S (in Ref. 1; CAA57202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29715 MW; ADA88A33D8A1079E CRC64;
MFDKHTHTLI AQRLDQAEKQ REQIRAISLD YPEITIEDAY AVQREWVRLK IAEGRTLKGH
KIGLTSKAMQ ASSQISEPDY GALLDDMFFH DGSDIPTDRF IVPRIEVELA FVLAKPLRGP
NCTLFDVYNA TDYVIPALEL IDARCHNIDP ETQRPRKVFD TISDNAANAG VILGGRPIKP
DELDLRWISA LMYRNGVIEE TGVAAGVLNH PANGVAWLAN KLAPYDVQLE AGQIILGGSF
TRPVPARKGD TFHVDYGNMG SISCRFV
