A8A345 (HCAF_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Protein existence	Inferred 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-phenylpropanoate + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+. HAMAP MF_01649 (2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + 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.
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred 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 – 172	172	3-phenylpropionate/cinnamic acid dioxygenase subunit beta HAMAP MF_01649		PRO_0000333712

Sequences

	Sequence		Length	Mass (Da)
	A8A345 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 58203B22B5D97554	FASTA	172	20,565
	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

References

[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]. Strain: HS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000802 Genomic DNA. Translation: ABV06949.1.
RefSeq	YP_001459332.1. NC_009800.1.
3D structure databases
ProteinModelPortal	A8A345.
SMR	A8A345. Positions 2-172.
ModBase	Search...
Protein-protein interaction databases
STRING	A8A345.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000052841; EBESCP00000050826; EBESCG00000051889.
GeneID	5595229.
GenomeReviews	Gene locus EcHS_A2691 in contig CP000802_GR.
KEGG	ecx:EcHS_A2691.
PATRIC	18315363. VBIEscCol77814_2636.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG5517.
HOGENOM	HOG000106036.
KO	K05709.
OMA	ARRTICV.
ProtClustDB	PRK10069.
Family and domain databases
HAMAP	MF_01649. HcaF. [Tree]
InterPro	IPR023712. HcaF. IPR000391. Rng_hydr_dOase-bsu. [Graphical view]
Pfam	PF00866. Ring_hydroxyl_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HCAF_ECOHS

Accession

Primary (citable) accession number: A8A345

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 23, 2007
Last modified:	May 16, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program