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B2N374 (B2N374_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-phenylpropionate/cinnamic acid dioxygenase subunit beta HAMAP MF_01649
EC=1.14.12.19 HAMAP MF_01649
Alternative name(s):
Digoxigenin subunit beta HAMAP MF_01649
Gene names
Name:hcaF HAMAP MF_01649 EMBL EDU66160.1
ORF Names:Ec53638_3452 EMBL EDU66160.1
OrganismEscherichia coli 53638 EMBL EDU66160.1
Taxonomic identifier344610 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 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. HAMAP MF_01649

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Sequences

Sequence LengthMass (Da)Tools
B2N374 [UniParc].

Last modified July 1, 2008. 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

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References

[1]Rasko D.A., Rosovitz M.J., Brinkley C., Myers G.S.A., Seshadri R., Cer R.Z., Jiang L., Sebastian Y., Ravel J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 53638 EMBL EDU66160.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAKB02000001 Genomic DNA. Translation: EDU66160.1.

3D structure databases

ProteinModelPortalB2N374.
SMRB2N374. Positions 2-172.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC31213535. VBIEscCol26876_3786.

Family and domain databases

HAMAPMF_01649. HcaF.
[Tree]
InterProIPR023712. HcaF.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB2N374_ECOLX
AccessionPrimary (citable) accession number: B2N374
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: December 14, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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