P0ABR5 (HCAE_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 72.
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: 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha EC=1.14.12.19 Alternative name(s): Digoxigenin subunit alpha | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 453 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. Ref.5 |
| Catalytic activity | 3-phenylpropanoate + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+. HAMAP-Rule MF_01648 (2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+. HAMAP-Rule MF_01648 |
| Cofactor | Binds 1 2Fe-2S cluster Probable. Binds 1 iron ion Probable. |
| Pathway | Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01648 |
| Subunit structure | This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (HcaE and HcaF), a ferredoxin (HcaC) and a ferredoxin reductase (HcaD). |
| Sequence similarities | Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | 2Fe-2S Iron Iron-sulfur Metal-binding NAD |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | 3-phenylpropionate catabolic process Inferred from mutant phenotype PubMed 3531186PubMed 6345502. Source: EcoCyc |
| Molecular_function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3-phenylpropionate dioxygenase activityInferred from electronic annotation. Source: HAMAP iron ion bindingInferred from electronic annotation. Source: HAMAP oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 453 | 453 | 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha HAMAP-Rule MF_01648 | PRO_0000085061 | |||||
Regions | |||||||||
| Domain | 44 – 142 | 99 | Rieske | ||||||
Sites | |||||||||
| Metal binding | 85 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 87 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen By similarity | ||||||
| Metal binding | 105 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 108 | 1 | Iron-sulfur (2Fe-2S); via pros nitrogen By similarity | ||||||
| Metal binding | 213 | 1 | Iron By similarity | ||||||
| Metal binding | 218 | 1 | Iron By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 20 | 1 | V → A in CAA86018. Ref.1 | ||||||
| Sequence conflict | 384 – 453 | 70 | GHRAR…QEVMK → ATAPATANCVWKWGLVRKSA ATTAFLALLTISFQKLPLVE CTNAGPIF in CAA86018. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Turlin E., Gasser F., Biville F. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T.DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12." Diaz E., Ferrandez A., Garcia J.L. J. Bacteriol. 180:2915-2923(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z37966 Genomic DNA. Translation: CAA86018.1. U00096 Genomic DNA. Translation: AAC75591.1. AP009048 Genomic DNA. Translation: BAA16441.1. |
| PIR | A65031. |
| RefSeq | NP_417033.1. NC_000913.2. YP_490766.1. NC_007779.1. |
3D structure databases | |
| ProteinModelPortal | P0ABR5. |
| SMR | P0ABR5. Positions 9-434. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P0ABR5. 5 interactions. |
| STRING | 511145.b2538. |
Proteomic databases | |
| PRIDE | P0ABR5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC75591; AAC75591; b2538. BAA16441; BAA16441; BAA16441. |
| GeneID | 12932583. 946998. |
| KEGG | ecj:Y75_p2491. eco:b2538. |
| PATRIC | 32120473. VBIEscCol129921_2639. |
Organism-specific databases | |
| EchoBASE | EB3229. |
| EcoGene | EG13456. hcaE. |
Phylogenomic databases | |
| eggNOG | COG4638. |
| HOGENOM | HOG000105925. |
| KO | K05708. |
| OMA | FRIARNM. |
| ProtClustDB | CLSK880425. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:PHENYLPRODIOXY-MONOMER. ECOL316407:JW2522-MONOMER. MetaCyc:PHENYLPRODIOXY-MONOMER. |
| UniPathway | UPA00714. |
Gene expression databases | |
| Genevestigator | P0ABR5. |
Family and domain databases | |
| Gene3D | 2.102.10.10. 1 hit. 3.90.380.10. 1 hit. |
| HAMAP | MF_01648. HcaE. |
| InterPro | IPR020875. HcaE. IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C_dom. IPR001663. Rng_hydr_dOase-A. [Graphical view] |
| Pfam | PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view] |
| PRINTS | PR00090. RNGDIOXGNASE. |
| SUPFAM | SSF50022. Rieske_dom. 1 hit. |
| PROSITE | PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HCAE_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0ABR5 Secondary accession number(s): P77590, P78203, Q47139 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
