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P37352

- HPCE_ECOLX

UniProt

P37352 - HPCE_ECOLX

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Protein

Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase

Gene

hpcE

Organism
Escherichia coli
Status
Reviewed - 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 = 5-carboxy-2-oxohept-3-enedioate.
5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2.

Cofactori

Mg2+1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi276 – 2761Divalent metal cation
Metal bindingi278 – 2781Divalent metal cation
Metal bindingi307 – 3071Divalent metal cation

GO - Molecular functioni

  1. 5-carboxymethyl-2-hydroxymuconate delta-isomerase activity Source: UniProtKB-EC
  2. 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 4-hydroxyphenylacetate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

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 isomerase (EC:5.3.3.10)
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:4.1.1.68)
Alternative name(s):
5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
Short name:
OPET decarboxylase
Gene namesi
Name:hpcE
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Homoprotocatechuate catabolism bifunctional isomerase/decarboxylasePRO_0000156835Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi13 – 197Combined sources
Helixi22 – 243Combined sources
Turni26 – 283Combined sources
Beta strandi36 – 405Combined sources
Helixi42 – 443Combined sources
Beta strandi52 – 543Combined sources
Beta strandi56 – 583Combined sources
Beta strandi64 – 707Combined sources
Beta strandi74 – 763Combined sources
Helixi79 – 857Combined sources
Beta strandi86 – 938Combined sources
Beta strandi102 – 1043Combined sources
Helixi107 – 1104Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi139 – 1457Combined sources
Helixi146 – 1483Combined sources
Beta strandi149 – 1513Combined sources
Helixi153 – 1619Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi199 – 2057Combined sources
Helixi206 – 2083Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi249 – 2524Combined sources
Helixi254 – 2563Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi277 – 2837Combined sources
Beta strandi287 – 2893Combined sources
Turni292 – 2943Combined sources
Helixi295 – 2984Combined sources
Beta strandi299 – 3068Combined sources
Helixi311 – 3133Combined sources
Beta strandi316 – 3205Combined sources
Helixi322 – 3254Combined sources
Beta strandi331 – 3333Combined sources
Helixi340 – 3423Combined sources
Beta strandi350 – 3556Combined sources
Beta strandi358 – 3647Combined sources
Helixi365 – 3673Combined sources
Beta strandi368 – 3703Combined sources
Helixi372 – 3809Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi405 – 4106Combined sources
Turni411 – 4133Combined sources
Beta strandi414 – 4229Combined sources
Helixi423 – 4264Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP37352.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 202202ApproximateAdd
BLAST
Repeati203 – 405203ApproximateAdd
BLAST

Sequence similaritiesi

Belongs to the FAH family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di3.90.850.10. 2 hits.
InterProiIPR002529. Fumarylacetoacetase_C.
IPR011234. 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 .
PIRi S38348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GTT X-ray 1.70 A/B/C/D 1-427 [» ]
1I7O X-ray 1.70 A/B/C/D 1-427 [» ]
ProteinModelPortali P37352.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00208 ; UER00419 .
UPA00208 ; UER00420 .

Miscellaneous databases

EvolutionaryTracei P37352.

Family and domain databases

Gene3Di 3.90.850.10. 2 hits.
InterProi IPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR012684. HPA_isomer/decarb_C.
IPR012686. HPA_isomer/decarb_N.
[Graphical view ]
Pfami PF01557. FAA_hydrolase. 2 hits.
[Graphical view ]
SUPFAMi SSF56529. SSF56529. 2 hits.
TIGRFAMsi TIGR02303. HpaG-C-term. 1 hit.
TIGR02305. HpaG-N-term. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C."
    Roper D.I., Cooper R.A.
    Eur. J. Biochem. 217:575-580(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION.
    Strain: C.
  2. Roper D.I.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression."
    Roper D.I., Fawcett T., Cooper R.A.
    Mol. Gen. Genet. 237:241-250(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
    Strain: C.
  4. "The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold."
    Tame J.R.H., Namba K., Dodson E.J., Roper D.I.
    Biochemistry 41:2982-2989(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT, COFACTOR.

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 26, 2014
This is version 74 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

External Data

Dasty 3