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Protein

5-carboxymethyl-2-hydroxymuconate Delta-isomerase

Gene

hpcD

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

Functioni

Transforms 5-carboxymethyl-2-hydroxy-muconic acid (CHM) into 5-oxo-pent-3-ene-1,2,5-tricarboxylic acid (OPET).

Catalytic activityi

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

pH dependencei

Optimum pH is 7.6.1 Publication

Pathwayi: 4-hydroxyphenylacetate degradation

This protein is involved in step 4 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. 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase (hpaG), 5-carboxymethyl-2-hydroxymuconate Delta-isomerase (hpcD), 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
Active sitei2Proton acceptor; via imino nitrogen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

UniPathwayiUPA00208; UER00419.

Names & Taxonomyi

Protein namesi
Recommended name:
5-carboxymethyl-2-hydroxymuconate Delta-isomerase (EC:5.3.3.101 Publication)
Alternative name(s):
5-carboxymethyl-2-hydroxymuconic acid isomerase1 Publication
Short name:
CHM isomerase1 Publication
Short name:
CHMI
Gene namesi
Name:hpcD
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000840412 – 1265-carboxymethyl-2-hydroxymuconate Delta-isomeraseAdd BLAST125

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

Secondary structure

1126
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi10 – 12Combined sources3
Helixi13 – 16Combined sources4
Helixi18 – 30Combined sources13
Beta strandi33 – 35Combined sources3
Helixi37 – 39Combined sources3
Beta strandi41 – 52Combined sources12
Beta strandi59 – 68Combined sources10
Helixi74 – 91Combined sources18
Helixi93 – 96Combined sources4
Beta strandi99 – 109Combined sources11
Beta strandi112 – 119Combined sources8
Helixi120 – 124Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OTGX-ray2.10A/B/C2-126[»]
ProteinModelPortaliQ05354.
SMRiQ05354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05354.

Family & Domainsi

Family and domain databases

CDDicd00580. CHMI. 1 hit.
InterProiIPR004220. 5-COMe_2-OHmuconate_Isoase.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PfamiPF02962. CHMI. 1 hit.
[Graphical view]
SUPFAMiSSF55331. SSF55331. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05354-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHFIVECSD NIREEADLPG LFAKVNPTLA ATGIFPLAGI RSRVHWVDTW
60 70 80 90 100
QMADGQHDYA SVHMTLKIGA GRSLESRQQA GEMLFELIKT HFAALMESRL
110 120
LALSFEIEEL HPTLNFKQNN VHALFK
Length:126
Mass (Da):14,215
Last modified:January 23, 2007 - v3
Checksum:i7494E625A76BBCEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53666 Genomic DNA. Translation: CAA37707.1.
X55200 Genomic DNA. Translation: CAA38986.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53666 Genomic DNA. Translation: CAA37707.1.
X55200 Genomic DNA. Translation: CAA38986.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OTGX-ray2.10A/B/C2-126[»]
ProteinModelPortaliQ05354.
SMRiQ05354.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00208; UER00419.

Miscellaneous databases

EvolutionaryTraceiQ05354.

Family and domain databases

CDDicd00580. CHMI. 1 hit.
InterProiIPR004220. 5-COMe_2-OHmuconate_Isoase.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PfamiPF02962. CHMI. 1 hit.
[Graphical view]
SUPFAMiSSF55331. SSF55331. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHPCD_ECOLX
AccessioniPrimary (citable) accession number: Q05354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

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.