HPCE_ECOLX
ID HPCE_ECOLX Reviewed; 427 AA.
AC P37352;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase;
DE Includes:
DE RecName: Full=2-hydroxyhepta-2,4-diene-1,7-dioate isomerase {ECO:0000303|PubMed:8223600};
DE Short=HHDD isomerase;
DE EC=5.3.3.10 {ECO:0000269|PubMed:8223600};
DE AltName: Full=5-carboxymethyl-2-hydroxymuconate Delta-isomerase;
DE Includes:
DE RecName: Full=5-carboxymethyl-2-oxo-hex-3-ene-1,7-dioate decarboxylase;
DE EC=4.1.1.68 {ECO:0000269|PubMed:8223600};
DE AltName: Full=5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase {ECO:0000303|PubMed:8223600};
DE Short=OPET decarboxylase;
GN Name=hpcE;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=C;
RX PubMed=8223600; DOI=10.1111/j.1432-1033.1993.tb18279.x;
RA Roper D.I., Cooper R.A.;
RT "Purification, nucleotide sequence and some properties of a bifunctional
RT isomerase/decarboxylase from the homoprotocatechuate degradative pathway of
RT Escherichia coli C.";
RL Eur. J. Biochem. 217:575-580(1993).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Roper D.I.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RC STRAIN=C;
RX PubMed=8384293; DOI=10.1007/bf00282806;
RA Roper D.I., Fawcett T., Cooper R.A.;
RT "The Escherichia coli C homoprotocatechuate degradative operon: hpc gene
RT order, direction of transcription and control of expression.";
RL Mol. Gen. Genet. 237:241-250(1993).
RN [4] {ECO:0007744|PDB:1GTT}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT, AND COFACTOR.
RX PubMed=11863436; DOI=10.1021/bi015717t;
RA Tame J.R.H., Namba K., Dodson E.J., Roper D.I.;
RT "The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with
RT a multifunctional fold.";
RL Biochemistry 41:2982-2989(2002).
CC -!- FUNCTION: Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic
CC acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it
CC to OHED (2-oxo-hept-3-ene-1,7-dioate). {ECO:0000269|PubMed:8223600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate =
CC (3E,5R)-5-carboxy-2-oxohept-3-enedioate; Xref=Rhea:RHEA:18813,
CC ChEBI:CHEBI:47961, ChEBI:CHEBI:87491; EC=5.3.3.10;
CC Evidence={ECO:0000269|PubMed:8223600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5R)-5-carboxy-2-oxohept-3-enedioate + H(+) = (4Z)-2-
CC oxohept-4-enedioate + CO2; Xref=Rhea:RHEA:14397, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:87491, ChEBI:CHEBI:87507; EC=4.1.1.68;
CC Evidence={ECO:0000269|PubMed:8223600};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11863436};
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 4/7.
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 5/7.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11863436,
CC ECO:0000269|PubMed:8223600}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; X75028; CAA52936.2; -; Genomic_DNA.
DR EMBL; S56952; AAB25803.1; -; Genomic_DNA.
DR PIR; S38348; S38348.
DR PDB; 1GTT; X-ray; 1.70 A; A/B/C/D=1-427.
DR PDB; 1I7O; X-ray; 1.70 A; A/B/C/D=1-427.
DR PDBsum; 1GTT; -.
DR PDBsum; 1I7O; -.
DR AlphaFoldDB; P37352; -.
DR SMR; P37352; -.
DR BRENDA; 4.1.1.68; 2026.
DR UniPathway; UPA00208; UER00419.
DR UniPathway; UPA00208; UER00420.
DR EvolutionaryTrace; P37352; -.
DR GO; GO:0008704; F:5-carboxymethyl-2-hydroxymuconate delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0018800; F:5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901023; P:4-hydroxyphenylacetate catabolic process; IEA:InterPro.
DR Gene3D; 3.90.850.10; -; 2.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR InterPro; IPR012684; HPA_isomer/decarb_C.
DR InterPro; IPR012686; HPA_isomer/decarb_N.
DR Pfam; PF01557; FAA_hydrolase; 2.
DR SUPFAM; SSF56529; SSF56529; 2.
DR TIGRFAMs; TIGR02303; HpaG-C-term; 1.
DR TIGRFAMs; TIGR02305; HpaG-N-term; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Calcium;
KW Direct protein sequencing; Isomerase; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Repeat.
FT CHAIN 1..427
FT /note="Homoprotocatechuate catabolism bifunctional
FT isomerase/decarboxylase"
FT /id="PRO_0000156835"
FT REPEAT 1..202
FT /note="Approximate"
FT REPEAT 203..405
FT /note="Approximate"
FT BINDING 276
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0007744|PDB:1GTT, ECO:0007744|PDB:1I7O"
FT BINDING 278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0007744|PDB:1GTT, ECO:0007744|PDB:1I7O"
FT BINDING 307
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0007744|PDB:1GTT, ECO:0007744|PDB:1I7O"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1GTT"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1I7O"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1GTT"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:1GTT"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:1GTT"
FT STRAND 414..422
FT /evidence="ECO:0007829|PDB:1GTT"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:1GTT"
SQ SEQUENCE 427 AA; 46878 MW; D4CF62027017B295 CRC64;
MKGTIFAVAL NHRSQLDAWQ EAFQQSPIKA PPKTAVWFIK PRNTVIGCGE PIPFPQGENL
LSGATVALIV GKTATKVREE DAAEYIAGYA LANDVSLPEE SFYRPAIKAK CRDGFCPIGE
TVALSNVDNL TIYTEINGRP ADHWNTSDLQ RNAAQLLSAL SEFATLNPGD AILLGTPQAR
VEIQPGDRVR VLAEGFPPLE NPVVDEREVT TRKSFPTLPH PHGTLFALGL NYADHASELE
FKPPEEPLVF LKAPNTLTGD NQTSVRPNNI EYMHYEAELV VVIGKQARNV SEADAMDYVA
GYTVCNDYAI RDYLENYYRP NLRVKSRDGL TPMLSTIVPK EAIPDPHNLT LRTFVNGELR
QQGTTADLIF SVPFLIAYLS EFMTLNPGDM IATGTPKGLS DVGDEVVVEV EGVGRLVNRI
VSEETAK
