NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/1471-2164-7-173; PubMed=16822325 [NCBI, ExPASy, EBI, Israel, Japan]
Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
"Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a.";
BMC Genomics 7:173-173(2006).

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).
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) (By similarity).
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

CP000266; ABF04685.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_689990.1; -.

3D structure databases

ModBase

Q0T1Y0.

Enzyme and pathway databases

BioCyc

SFLE373384:SFV_2587-MON; -.

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

Q0T1Y0.

Genome annotation databases

GeneID

4207322; -.

GenomeReviews

CP000266_GR; SFV_2587.

KEGG

sfv:SFV_2587; -.

Phylogenomic databases

HOGENOM

Q0T1Y0; -.

Genome annotation databases

CMR

Q0T1Y0; SFV_2587.

Other

ProtoNet

Q0T1Y0.

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_0000333716`

Sequence information

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

Molecular weight: 20613 Da [This is the MW of the unprocessed precursor]

CRC64: 582027F378D97554 [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 NCQVSETDIP NVFAVRVNYL 

       130        140        150        160        170 
LYRAQKERDE TFYVGTRFDK VRRLEYDNWR LLERDIVLDQ AVITSHNLSV LF

Q0T1Y0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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