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Q05354

- HPCD_ECOLX

UniProt

Q05354 - HPCD_ECOLX

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Protein

5-carboxymethyl-2-hydroxymuconate Delta-isomerase

Gene
hpcD
Organism
Escherichia coli
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Proton acceptor; via imino nitrogen

GO - Molecular functioni

  1. 5-carboxymethyl-2-hydroxymuconate delta-isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
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 – 97
Helixi10 – 123
Helixi13 – 164
Helixi18 – 3013
Beta strandi33 – 353
Helixi37 – 393
Beta strandi41 – 5212
Beta strandi59 – 6810
Helixi74 – 9118
Helixi93 – 964
Beta strandi99 – 10911
Beta strandi112 – 1198
Helixi120 – 1245

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTGX-ray2.10A/B/C2-126[»]
ProteinModelPortaliQ05354.
SMRiQ05354. Positions 2-126.

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

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MPHFIVECSD NIREEADLPG LFAKVNPTLA ATGIFPLAGI RSRVHWVDTW    50
QMADGQHDYA SVHMTLKIGA GRSLESRQQA GEMLFELIKT HFAALMESRL 100
LALSFEIEEL HPTLNFKQNN VHALFK 126
Length:126
Mass (Da):14,215
Last modified:January 23, 2007 - v3
Checksum:i7494E625A76BBCEC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53666 Genomic DNA. Translation: CAA37707.1.
X55200 Genomic DNA. Translation: CAA38986.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53666 Genomic DNA. Translation: CAA37707.1 .
X55200 Genomic DNA. Translation: CAA38986.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OTG X-ray 2.10 A/B/C 2-126 [» ]
ProteinModelPortali Q05354.
SMRi Q05354. Positions 2-126.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00208 ; UER00419 .

Miscellaneous databases

EvolutionaryTracei Q05354.

Family and domain databases

InterProi IPR004220. 5-COMe_2-OHmuconate_Isoase.
IPR014347. Tautomerase/MIF_sf.
[Graphical view ]
Pfami PF02962. CHMI. 1 hit.
[Graphical view ]
SUPFAMi SSF55331. SSF55331. 1 hit.
ProtoNeti Search...

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: October 16, 2013
This is version 69 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

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