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

Pathway: 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-hepta-3-ene-1,7-dioic acid hydratase (hpcG)
  7. 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 (hpcH), 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 (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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Proton acceptor; via imino nitrogen

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:5.3.3.10)
Alternative name(s):
5-carboxymethyl-2-hydroxymuconic acid isomerase
Short name:
CHM isomerase
Short name:
CHMI
Gene namesi
Name:hpcD
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 1261255-carboxymethyl-2-hydroxymuconate Delta-isomerasePRO_0000084041Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi10 – 123Combined sources
Helixi13 – 164Combined sources
Helixi18 – 3013Combined sources
Beta strandi33 – 353Combined sources
Helixi37 – 393Combined sources
Beta strandi41 – 5212Combined sources
Beta strandi59 – 6810Combined sources
Helixi74 – 9118Combined sources
Helixi93 – 964Combined sources
Beta strandi99 – 10911Combined sources
Beta strandi112 – 1198Combined sources
Helixi120 – 1245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTGX-ray2.10A/B/C2-126[»]
ProteinModelPortaliQ05354.
SMRiQ05354. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05354.

Family & Domainsi

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTGX-ray2.10A/B/C2-126[»]
ProteinModelPortaliQ05354.
SMRiQ05354. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00208; UER00419.

Miscellaneous databases

EvolutionaryTraceiQ05354.

Family and domain databases

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

Publicationsi

  1. "Purification, some properties and nucleotide sequence of 5-carboxymethyl-2-hydroxymuconate isomerase of Escherichia coli C."
    Roper D.I., Cooper R.A.
    FEBS Lett. 266:63-66(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C.
  2. "Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C."
    Roper D.I., Cooper R.A.
    FEBS Lett. 275:53-57(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    Strain: C.
  3. "Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases."
    Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J., Wilson K.S., Wigley D.B.
    Biochemistry 35:792-802(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

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 26, 2014
This is version 70 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

Documents

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

External Data

Dasty 3

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 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.