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Protein

Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase

Gene

hpcE

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it to OHED (2-oxo-hept-3-ene-1,7-dioate).1 Publication

Catalytic activityi

5-carboxymethyl-2-hydroxymuconate = (3E,5R)-5-carboxy-2-oxohept-3-enedioate.1 Publication
(3E,5R)-5-carboxy-2-oxohept-3-enedioate = (4Z)-2-oxohept-4-enedioate + CO2.1 Publication

Cofactori

Mg2+1 Publication

Pathwayi: 4-hydroxyphenylacetate degradation

This protein is involved in step 4 and 5 of the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. 4-hydroxyphenylacetate 3-monooxygenase oxygenase component (hpaB), 4-hydroxyphenylacetate 3-monooxygenase reductase component (hpaC)
  2. 3,4-dihydroxyphenylacetate 2,3-dioxygenase (hpcB)
  3. 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase (hpcC)
  4. 5-carboxymethyl-2-hydroxymuconate Delta-isomerase (hpcD), 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase (hpaG), Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase (hpcE)
  5. 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase (hpaG), Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase (hpcE)
  6. 2-oxo-hept-4-ene-1,7-dioate hydratase (hpcG)
  7. 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (yfaU), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH)
This subpathway is part of the pathway 4-hydroxyphenylacetate degradation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate, the pathway 4-hydroxyphenylacetate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi276Divalent metal cation1
Metal bindingi278Divalent metal cation1
Metal bindingi307Divalent metal cation1

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.1.1.68. 2026.
UniPathwayiUPA00208; UER00419.
UPA00208; UER00420.

Names & Taxonomyi

Protein namesi
Recommended name:
Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase
Including the following 2 domains:
2-hydroxyhepta-2,4-diene-1,7-dioate isomerase1 Publication (EC:5.3.3.101 Publication)
Short name:
HHDD isomerase
Alternative name(s):
5-carboxymethyl-2-hydroxymuconate Delta-isomerase
5-carboxymethyl-2-oxo-hex-3-ene-1,7-dioate decarboxylase (EC:4.1.1.681 Publication)
Alternative name(s):
5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase1 Publication
Short name:
OPET decarboxylase
Gene namesi
Name:hpcE
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001568351 – 427Homoprotocatechuate catabolism bifunctional isomerase/decarboxylaseAdd BLAST427

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi469008.ECD_04230.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi13 – 19Combined sources7
Helixi22 – 24Combined sources3
Turni26 – 28Combined sources3
Beta strandi36 – 40Combined sources5
Helixi42 – 44Combined sources3
Beta strandi52 – 54Combined sources3
Beta strandi56 – 58Combined sources3
Beta strandi64 – 70Combined sources7
Beta strandi74 – 76Combined sources3
Helixi79 – 85Combined sources7
Beta strandi86 – 93Combined sources8
Beta strandi102 – 104Combined sources3
Helixi107 – 110Combined sources4
Beta strandi116 – 118Combined sources3
Beta strandi131 – 136Combined sources6
Beta strandi139 – 145Combined sources7
Helixi146 – 148Combined sources3
Beta strandi149 – 151Combined sources3
Helixi153 – 161Combined sources9
Beta strandi171 – 173Combined sources3
Beta strandi188 – 193Combined sources6
Beta strandi199 – 205Combined sources7
Helixi206 – 208Combined sources3
Beta strandi219 – 221Combined sources3
Beta strandi225 – 230Combined sources6
Beta strandi249 – 252Combined sources4
Helixi254 – 256Combined sources3
Beta strandi262 – 266Combined sources5
Beta strandi277 – 283Combined sources7
Beta strandi287 – 289Combined sources3
Turni292 – 294Combined sources3
Helixi295 – 298Combined sources4
Beta strandi299 – 306Combined sources8
Helixi311 – 313Combined sources3
Beta strandi316 – 320Combined sources5
Helixi322 – 325Combined sources4
Beta strandi331 – 333Combined sources3
Helixi340 – 342Combined sources3
Beta strandi350 – 355Combined sources6
Beta strandi358 – 364Combined sources7
Helixi365 – 367Combined sources3
Beta strandi368 – 370Combined sources3
Helixi372 – 380Combined sources9
Beta strandi390 – 392Combined sources3
Beta strandi405 – 410Combined sources6
Turni411 – 413Combined sources3
Beta strandi414 – 422Combined sources9
Helixi423 – 426Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GTTX-ray1.70A/B/C/D1-427[»]
1I7OX-ray1.70A/B/C/D1-427[»]
ProteinModelPortaliP37352.
SMRiP37352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37352.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1 – 202ApproximateAdd BLAST202
Repeati203 – 405ApproximateAdd BLAST203

Sequence similaritiesi

Belongs to the FAH family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105ERH. Bacteria.
COG0179. LUCA.

Family and domain databases

Gene3Di3.90.850.10. 2 hits.
InterProiIPR011234. Fumarylacetoacetase_C-rel.
IPR012684. HPA_isomer/decarb_C.
IPR012686. HPA_isomer/decarb_N.
[Graphical view]
PfamiPF01557. FAA_hydrolase. 2 hits.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 2 hits.
TIGRFAMsiTIGR02303. HpaG-C-term. 1 hit.
TIGR02305. HpaG-N-term. 1 hit.

Sequencei

Sequence statusi: Complete.

P37352-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGTIFAVAL NHRSQLDAWQ EAFQQSPIKA PPKTAVWFIK PRNTVIGCGE
60 70 80 90 100
PIPFPQGENL LSGATVALIV GKTATKVREE DAAEYIAGYA LANDVSLPEE
110 120 130 140 150
SFYRPAIKAK CRDGFCPIGE TVALSNVDNL TIYTEINGRP ADHWNTSDLQ
160 170 180 190 200
RNAAQLLSAL SEFATLNPGD AILLGTPQAR VEIQPGDRVR VLAEGFPPLE
210 220 230 240 250
NPVVDEREVT TRKSFPTLPH PHGTLFALGL NYADHASELE FKPPEEPLVF
260 270 280 290 300
LKAPNTLTGD NQTSVRPNNI EYMHYEAELV VVIGKQARNV SEADAMDYVA
310 320 330 340 350
GYTVCNDYAI RDYLENYYRP NLRVKSRDGL TPMLSTIVPK EAIPDPHNLT
360 370 380 390 400
LRTFVNGELR QQGTTADLIF SVPFLIAYLS EFMTLNPGDM IATGTPKGLS
410 420
DVGDEVVVEV EGVGRLVNRI VSEETAK
Length:427
Mass (Da):46,878
Last modified:March 1, 2004 - v2
Checksum:iD4CF62027017B295
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75028 Genomic DNA. Translation: CAA52936.2.
S56952 Genomic DNA. Translation: AAB25803.1.
PIRiS38348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75028 Genomic DNA. Translation: CAA52936.2.
S56952 Genomic DNA. Translation: AAB25803.1.
PIRiS38348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GTTX-ray1.70A/B/C/D1-427[»]
1I7OX-ray1.70A/B/C/D1-427[»]
ProteinModelPortaliP37352.
SMRiP37352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi469008.ECD_04230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105ERH. Bacteria.
COG0179. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00208; UER00419.
UPA00208; UER00420.
BRENDAi4.1.1.68. 2026.

Miscellaneous databases

EvolutionaryTraceiP37352.

Family and domain databases

Gene3Di3.90.850.10. 2 hits.
InterProiIPR011234. Fumarylacetoacetase_C-rel.
IPR012684. HPA_isomer/decarb_C.
IPR012686. HPA_isomer/decarb_N.
[Graphical view]
PfamiPF01557. FAA_hydrolase. 2 hits.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 2 hits.
TIGRFAMsiTIGR02303. HpaG-C-term. 1 hit.
TIGR02305. HpaG-N-term. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHPCE_ECOLX
AccessioniPrimary (citable) accession number: P37352
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: March 1, 2004
Last modified: November 2, 2016
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.