Reviewed, UniProtKB/Swiss-Prot Q47140 (HCAF_ECOLI)

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
Synonyms:	digB, hcaA2, hcaB, phdC2, yfhV
Ordered Locus Names:	b2539, JW2523

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	172 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. Ref.5
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-phenylpropionic acid 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). HAMAP MF_01649
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: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: HAMAP 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_0000085077
Experimental info
	Sequence conflict	11	1	H → Y in CAA86019. Ref.4
	Sequence conflict	49	1	N → D in CAA86019. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q47140-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 83833B22A75BE546	FASTA	172	20,579
	10 20 30 40 50 60 MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLAQLDEEI RYTMRTTVNA 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	Turlin E., Gasser F., Biville F. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49. Strain: K12.
[5]	"Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12." Diaz E., Ferrandez A., Garcia J.L. J. Bacteriol. 180:2915-2923(1998) [PubMed: 9603882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-172, FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00096 Genomic DNA. Translation: AAC75592.1. AP009048 Genomic DNA. Translation: BAA16442.1. Z37966 Genomic DNA. Translation: CAA86019.1. Y11070 Genomic DNA. Translation: CAA71949.1.
PIR	B65031.
RefSeq	AP_003125.1. NP_417034.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	946997.
GenomeReviews	Gene locus JW2523 in contig AP009048_GR. Gene locus b2539 in contig U00096_GR.
KEGG	ecj:JW2523. eco:b2539.
Organism-specific databases
EchoBASE	EB3230.
EcoGene	EG13457. hcaF.
CMR	Search...
Phylogenomic databases
HOGENOM	Q47140.
OMA	Q47140. DIFAGER.
Enzyme and pathway databases
BioCyc	EcoCyc:HCAA2-MON. MetaCyc:HCAA2-MON.
Family and domain databases
HAMAP	MF_01649. [Tree]
InterPro	IPR000391. Rng_hydr_dOase-bsu. [Graphical view]
Pfam	PF00866. Ring_hydroxyl_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HCAF_ECOLI

Accession

Primary (citable) accession number: Q47140
Secondary accession number(s): P77508

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 5, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)