[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; DNA Res. 4:91-113(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49. STRAIN=K12; Turlin E., Gasser F., Biville F.; Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-172, AND FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS. STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140; PubMed=9603882 [NCBI, ExPASy, EBI, Israel, Japan] Diaz E., Ferrandez A., Garcia J.L.; "Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12."; J. Bacteriol. 180:2915-2923(1998).

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.
CATALYTIC ACTIVITY: 3-phenylpropanoic acid + NADH + O₂ = cis-3-(2-carboxyethyl)-3,5-cyclohexadiene-1,2-diol + NAD⁺.
CATALYTIC ACTIVITY: Cinnamic acid + H⁺ + NADH + O₂ = cis-3-(2-carboxyethenyl)-3,5-cyclohexadiene-1,2-diol + NAD⁺.
PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid degradation .
SUBUNIT: 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).
SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U00096; AAC75592.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16442.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z37966; CAA86019.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11070; CAA71949.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B65031; B65031.

RefSeq

AP_003125.1; -.
NP_417034.1; -.

3D structure databases

ModBase

Q47140.

Enzyme and pathway databases

BioCyc

EcoCyc:HCAA2-MON; -.
MetaCyc:HCAA2-MON; -.

Organism-specific databases

EchoBASE

EB3230; -.

EcoGene

EG13457; hcaF.

Ontologies

GO:0008695;	Molecular function: 3-phenylpropionate dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01649; -; 1.
PBIL [Tree]

InterPro

IPR000391; Rng_hydr_dOase-B.
Graphical view of domain structure.

Pfam

PF00866; Ring_hydroxyl_B; 1.
Pfam graphical view of domain structure.

BLOCKS

Q47140.

Genome annotation databases

GeneID

946997; -.

GenomeReviews

U00096_GR; b2539.
AP009048_GR; JW2523.

KEGG

ecj:JW2523; -.
eco:b2539; -.

Phylogenomic databases

HOGENOM

Q47140; -.

Genome annotation databases

CMR

Q47140; b2539.

Other

ProtoNet

Q47140.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 172`	`172`	`3-phenylpropionate/cinnamic acid dioxygenase subunit beta.`	`PRO_0000085077`
`CONFLICT`	`11 11`		`H -> Y (in Ref. 4; CAA86019).`
`CONFLICT`	`49 49`		`N -> D (in Ref. 4; CAA86019).`

Sequence information

Length: 172 AA [This is the length of the unprocessed precursor]

Molecular weight: 20579 Da [This is the MW of the unprocessed precursor]

CRC64: 83833B22A75BE546 [This is a checksum on the sequence]

        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

Q47140 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools