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P37352 (HPCE_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase

Including the following 2 domains:

  1. 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase
    Short name=HHDD isomerase
    EC=5.3.3.10
    Alternative name(s):
    5-carboxymethyl-2-hydroxymuconate Delta-isomerase
  2. 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 names
Name:hpcE
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1

Catalytic activity

5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate.

5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2.

Cofactor

Magnesium. Ref.4

Pathway

Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 4/7.

Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 5/7.

Subunit structure

Monomer. Ref.4

Sequence similarities

Belongs to the FAH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase
PRO_0000156835

Regions

Repeat1 – 202202Approximate
Repeat203 – 405203Approximate

Sites

Metal binding2761Divalent metal cation
Metal binding2781Divalent metal cation
Metal binding3071Divalent metal cation

Secondary structure

........................................................................................ 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37352 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: D4CF62027017B295

FASTA42746,878
        10         20         30         40         50         60 
MKGTIFAVAL NHRSQLDAWQ EAFQQSPIKA PPKTAVWFIK PRNTVIGCGE PIPFPQGENL 

        70         80         90        100        110        120 
LSGATVALIV GKTATKVREE DAAEYIAGYA LANDVSLPEE SFYRPAIKAK CRDGFCPIGE 

       130        140        150        160        170        180 
TVALSNVDNL TIYTEINGRP ADHWNTSDLQ RNAAQLLSAL SEFATLNPGD AILLGTPQAR 

       190        200        210        220        230        240 
VEIQPGDRVR VLAEGFPPLE NPVVDEREVT TRKSFPTLPH PHGTLFALGL NYADHASELE 

       250        260        270        280        290        300 
FKPPEEPLVF LKAPNTLTGD NQTSVRPNNI EYMHYEAELV VVIGKQARNV SEADAMDYVA 

       310        320        330        340        350        360 
GYTVCNDYAI RDYLENYYRP NLRVKSRDGL TPMLSTIVPK EAIPDPHNLT LRTFVNGELR 

       370        380        390        400        410        420 
QQGTTADLIF SVPFLIAYLS EFMTLNPGDM IATGTPKGLS DVGDEVVVEV EGVGRLVNRI 


VSEETAK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75028 Genomic DNA. Translation: CAA52936.2.
S56952 Genomic DNA. Translation: AAB25803.1.
PIRS38348.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GTTX-ray1.70A/B/C/D1-427[»]
1I7OX-ray1.70A/B/C/D1-427[»]
ProteinModelPortalP37352.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00208; UER00419.
UPA00208; UER00420.

Family and domain databases

Gene3D3.90.850.10. 2 hits.
InterProIPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR012684. HPA_isomer/decarb_C.
IPR012686. HPA_isomer/decarb_N.
[Graphical view]
PfamPF01557. FAA_hydrolase. 2 hits.
[Graphical view]
SUPFAMSSF56529. SSF56529. 2 hits.
TIGRFAMsTIGR02303. HpaG-C-term. 1 hit.
TIGR02305. HpaG-N-term. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37352.

Entry information

Entry nameHPCE_ECOLX
AccessionPrimary (citable) accession number: P37352
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways