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Reviewed, UniProtKB/Swiss-Prot A8A345 (HCAF_ECOHS)

Last modified June 15, 2010. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
3-phenylpropionate/cinnamic acid dioxygenase subunit beta

EC=1.14.12.19
Alternative name(s):
Digoxigenin subunit beta
Gene names
Name:hcaF
Ordered Locus Names:EcHS_A2691
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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Protein attributesHide

Sequence length172 AA.
Sequence statusComplete.
Protein existenceInferred from homology.
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General annotation (Comments)Hide

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 By similarity. HAMAP MF_01649

Catalytic activity

3-phenylpropanoic acid + NADH + O2 = cis-3-(2-carboxyethyl)-3,5-cyclohexadiene-1,2-diol + NAD+. HAMAP MF_01649

Cinnamic acid + H+ + NADH + O2 = cis-3-(2-carboxyethenyl)-3,5-cyclohexadiene-1,2-diol + NAD+. HAMAP MF_01649

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01649

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) By similarity. HAMAP MF_01649

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1721723-phenylpropionate/cinnamic acid dioxygenase subunit beta HAMAP MF_01649
PRO_0000333712
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SequencesHide

Sequence LengthMass (Da)Tools
A8A345-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 58203B22B5D97554

FASTA17220,565
        10         20         30         40         50         60 
MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA QTRDRRKGVQ 

        70         80         90        100        110        120 
PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQVSETDIP NVFAVRVNYL 

       130        140        150        160        170 
LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF 

« Hide

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ReferencesHide

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV06949.1.
RefSeqYP_001459332.1.

3D structure databases

SMRA8A345. Positions 8-171.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8A345.

Genome annotation databases

EnsemblBacteriaEBESCT00000052841; EBESCP00000050826; EBESCG00000051889.
GeneID5595229.
GenomeReviewsGene locus EcHS_A2691 in contig CP000802_GR.
KEGGecx:EcHS_A2691.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5517.
HOGENOMHBG582498.
OMAARRTICV.
ProtClustDBPRK10069.

Family and domain databases

HAMAPMF_01649. HcaF.
[Tree]
InterProIPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
ProtoNetSearch...
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Entry informationHide

Entry nameHCAF_ECOHS
AccessionPrimary (citable) accession number: A8A345
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: June 15, 2010
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents