B5Z112 (HCAF_ECO5E) 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:	ECH74115_3771

Organism

Escherichia coli O157:H7 (strain EC4115 / EHEC) [Complete proteome] [HAMAP]

Taxonomic identifier

444450 [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+. (2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+.
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_1000186973

Sequences

	Sequence		Length	Mass (Da)
	B5Z112 [UniParc]. Last modified November 25, 2008. Version 1. Checksum: 83962E2D02415546	FASTA	172	20,526
	10 20 30 40 50 60 MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI CYTMRTTVNA QTRDRRKGVQ 70 80 90 100 110 120 PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQISETDIP NVFAVRVNYL 130 140 150 160 170 LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF

References

[1]	"Complete genome sequence of Escherichia coli O157:H7 str. EC4115." Eppinger M., Sebastian Y., Ravel J. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: EC4115 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001164 Genomic DNA. Translation: ACI38933.1.
RefSeq	YP_002272013.1. NC_011353.1.
3D structure databases
ProteinModelPortal	B5Z112.
SMR	B5Z112. Positions 2-172.
ModBase	Search...
Protein-protein interaction databases
STRING	B5Z112.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000030895; EBESCP00000029598; EBESCG00000029945.
GeneID	6966724.
GenomeReviews	Gene locus ECH74115_3771 in contig CP001164_GR.
KEGG	ecf:ECH74115_3771.
PATRIC	18368190. VBIEscCol74651_3737.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011518.
HOGENOM	HBG582498.
OMA	ARRTICV.
ProtClustDB	PRK10069.
Family and domain databases
HAMAP	MF_01649. HcaF. [Tree]
InterPro	IPR023712. HcaF. IPR000391. Rng_hydr_dOase-bsu. [Graphical view]
KO	K05709.
Pfam	PF00866. Ring_hydroxyl_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HCAF_ECO5E

Accession

Primary (citable) accession number: B5Z112

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program