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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

Magnesium.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/decarboxylase
PRO_0000156835Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTTX-ray1.70A/B/C/D1-427[»]
1I7OX-ray1.70A/B/C/D1-427[»]
ProteinModelPortaliP37352.

Miscellaneous databases

EvolutionaryTraceiP37352.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the FAH family.

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

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MKGTIFAVAL NHRSQLDAWQ EAFQQSPIKA PPKTAVWFIK PRNTVIGCGE    50
PIPFPQGENL LSGATVALIV GKTATKVREE DAAEYIAGYA LANDVSLPEE 100
SFYRPAIKAK CRDGFCPIGE TVALSNVDNL TIYTEINGRP ADHWNTSDLQ 150
RNAAQLLSAL SEFATLNPGD AILLGTPQAR VEIQPGDRVR VLAEGFPPLE 200
NPVVDEREVT TRKSFPTLPH PHGTLFALGL NYADHASELE FKPPEEPLVF 250
LKAPNTLTGD NQTSVRPNNI EYMHYEAELV VVIGKQARNV SEADAMDYVA 300
GYTVCNDYAI RDYLENYYRP NLRVKSRDGL TPMLSTIVPK EAIPDPHNLT 350
LRTFVNGELR QQGTTADLIF SVPFLIAYLS EFMTLNPGDM IATGTPKGLS 400
DVGDEVVVEV EGVGRLVNRI VSEETAK 427
Length:427
Mass (Da):46,878
Last modified:March 1, 2004 - v2
Checksum:iD4CF62027017B295
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75028 Genomic DNA. Translation: CAA52936.2.
S56952 Genomic DNA. Translation: AAB25803.1.
PIRiS38348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75028 Genomic DNA. Translation: CAA52936.2 .
S56952 Genomic DNA. Translation: AAB25803.1 .
PIRi S38348.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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: October 16, 2013
This is version 72 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

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