Q05354 (HPCD_ECOLX) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||
| Organism | Escherichia coli | ||
| Taxonomic identifier | 562 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia![]() |
Protein attributes
| Sequence length | 126 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Transforms 5-carboxymethyl-2-hydroxy-muconic acid (CHM) into 5-oxo-pent-3-ene-1,2,5-tricarboxylic acid (OPET). |
| Catalytic activity | 5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate. |
| Pathway | |
| Subunit structure | Homotrimer. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Molecular function | Isomerase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological_process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | 5-carboxymethyl-2-hydroxymuconate delta-isomerase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | |||||||||||||||||||||||||||||
| Chain | 2 – 126 | 125 | 5-carboxymethyl-2-hydroxymuconate Delta-isomerase | PRO_0000084041 | ||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||
| Active site | 2 | 1 | Proton acceptor; via imino nitrogen | |||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Beta strand | 3 – 9 | 7 | ||||||||||||||||||||||||||||||
| Helix | 10 – 12 | 3 | ||||||||||||||||||||||||||||||
| Helix | 13 – 16 | 4 | ||||||||||||||||||||||||||||||
| Helix | 18 – 30 | 13 | ||||||||||||||||||||||||||||||
| Beta strand | 33 – 35 | 3 | ||||||||||||||||||||||||||||||
| Helix | 37 – 39 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 41 – 52 | 12 | ||||||||||||||||||||||||||||||
| Beta strand | 59 – 68 | 10 | ||||||||||||||||||||||||||||||
| Helix | 74 – 91 | 18 | ||||||||||||||||||||||||||||||
| Helix | 93 – 96 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 99 – 109 | 11 | ||||||||||||||||||||||||||||||
| Beta strand | 112 – 119 | 8 | ||||||||||||||||||||||||||||||
| Helix | 120 – 124 | 5 | ||||||||||||||||||||||||||||||
Sequences
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References
| [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). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X53666 Genomic DNA. Translation: CAA37707.1. X55200 Genomic DNA. Translation: CAA38986.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q05354. | ||||||||||||
| SMR | Q05354. Positions 2-126. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| UniPathway | UPA00208; UER00419. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR004220. 5-COMe_2-OHmuconate_Isoase. IPR014347. Tautomerase/MIF_sf. [Graphical view] | ||||||||||||
| Pfam | PF02962. CHMI. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF55331. SSF55331. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q05354. | ||||||||||||
Entry information
| Entry name | HPCD_ECOLX | ||||||||
| Accession | Primary (citable) accession number: Q05354 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |

Clusters with
