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Protein

3-phenylpropionate/cinnamic acid dioxygenase subunit beta

Gene

hcaF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

3-phenylpropanoate + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+.
(2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+.

Pathwayi: 3-phenylpropanoate degradation

This protein is involved in the pathway 3-phenylpropanoate degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway 3-phenylpropanoate degradation and in Aromatic compound metabolism.

GO - Molecular functioni

GO - Biological processi

  • 3-phenylpropionate catabolic process Source: EcoCyc
  • aromatic compound catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:HCAA2-MONOMER.
ECOL316407:JW2523-MONOMER.
MetaCyc:HCAA2-MONOMER.
UniPathwayiUPA00714.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phenylpropionate/cinnamic acid dioxygenase subunit beta (EC:1.14.12.19)
Gene namesi
Name:hcaF
Synonyms:digB, hcaA2, hcaB, phdC2, yfhV
Ordered Locus Names:b2539, JW2523
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13457. hcaF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000850771 – 1723-phenylpropionate/cinnamic acid dioxygenase subunit betaAdd BLAST172

Proteomic databases

PaxDbiQ47140.
PRIDEiQ47140.

Interactioni

Subunit structurei

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).

Protein-protein interaction databases

BioGridi4261576. 29 interactors.
STRINGi511145.b2539.

Structurei

3D structure databases

ProteinModelPortaliQ47140.
SMRiQ47140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108SBK. Bacteria.
COG5517. LUCA.
HOGENOMiHOG000106036.
InParanoidiQ47140.
KOiK05709.
OMAiQRHFISN.

Family and domain databases

CDDicd00667. ring_hydroxylating_dioxygenase. 1 hit.
Gene3Di3.10.450.50. 1 hit.
HAMAPiMF_01649. HcaF. 1 hit.
InterProiIPR023712. HcaF.
IPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.

Sequencei

Sequence statusi: Complete.

Q47140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA
60 70 80 90 100
QTRDRRKGVQ PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS
110 120 130 140 150
NCQISETDIP NVFAVRVNYL LYRAQKERDE TFYVGTRFDK VRRLEDDNWR
160 170
LLERDIVLDQ AVITSHNLSV LF
Length:172
Mass (Da):20,579
Last modified:November 1, 1997 - v2
Checksum:i83833B22A75BE546
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11H → Y in CAA86019 (Ref. 4) Curated1
Sequence conflicti49N → D in CAA86019 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75592.1.
AP009048 Genomic DNA. Translation: BAA16442.1.
Z37966 Genomic DNA. Translation: CAA86019.1.
Y11070 Genomic DNA. Translation: CAA71949.1.
PIRiB65031.
RefSeqiNP_417034.1. NC_000913.3.
WP_001276072.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75592; AAC75592; b2539.
BAA16442; BAA16442; BAA16442.
GeneIDi946997.
KEGGiecj:JW2523.
eco:b2539.
PATRICi32120475. VBIEscCol129921_2640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75592.1.
AP009048 Genomic DNA. Translation: BAA16442.1.
Z37966 Genomic DNA. Translation: CAA86019.1.
Y11070 Genomic DNA. Translation: CAA71949.1.
PIRiB65031.
RefSeqiNP_417034.1. NC_000913.3.
WP_001276072.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliQ47140.
SMRiQ47140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261576. 29 interactors.
STRINGi511145.b2539.

Proteomic databases

PaxDbiQ47140.
PRIDEiQ47140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75592; AAC75592; b2539.
BAA16442; BAA16442; BAA16442.
GeneIDi946997.
KEGGiecj:JW2523.
eco:b2539.
PATRICi32120475. VBIEscCol129921_2640.

Organism-specific databases

EchoBASEiEB3230.
EcoGeneiEG13457. hcaF.

Phylogenomic databases

eggNOGiENOG4108SBK. Bacteria.
COG5517. LUCA.
HOGENOMiHOG000106036.
InParanoidiQ47140.
KOiK05709.
OMAiQRHFISN.

Enzyme and pathway databases

UniPathwayiUPA00714.
BioCyciEcoCyc:HCAA2-MONOMER.
ECOL316407:JW2523-MONOMER.
MetaCyc:HCAA2-MONOMER.

Miscellaneous databases

PROiQ47140.

Family and domain databases

CDDicd00667. ring_hydroxylating_dioxygenase. 1 hit.
Gene3Di3.10.450.50. 1 hit.
HAMAPiMF_01649. HcaF. 1 hit.
InterProiIPR023712. HcaF.
IPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHCAF_ECOLI
AccessioniPrimary (citable) accession number: Q47140
Secondary accession number(s): P77508
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.