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 02-SEP-2026, entry version 106. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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:1901023; P:4-hydroxyphenylacetate catabolic process; IEA:InterPro. DR FunFam; 3.90.850.10:FF:000002; 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase; 1. DR Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 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 NCBIfam; TIGR02303; HpaG-C-term; 1. DR NCBIfam; TIGR02305; HpaG-N-term; 1. DR NCBIfam; NF011750; PRK15203.1; 1. DR PANTHER; PTHR11820:SF114; 4-HYDROXYPHENYLACETATE CATABOLISM PROTEIN; 1. DR PANTHER; PTHR11820; ACYLPYRUVASE; 1. DR Pfam; PF01557; FAA_hydrolase; 2. DR SUPFAM; SSF56529; FAH; 2. DR PDBsum; 1GTT; -. DR PDBsum; 1I7O; -. 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 HELIX 212..214 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 //