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⁺.
COFACTOR: Binds 1 iron ion (By similarity).
COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
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 alpha subunit family.
SIMILARITY: Contains 1 Rieske domain.

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; ABF04684.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_689989.1; -.

3D structure databases

ModBase

Q0T1Y1.

Ontologies

GO:0008695;	Molecular function: 3-phenylpropionate dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0005506;	Molecular function: iron ion binding (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_01648; -; 1.
PBIL [Tree]

InterPro

IPR005806; Rieske_reg.
IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879; Ring_hydroxy_dOase_asu_C.
IPR001663; Rng_hydr_dOase-A.
Graphical view of domain structure.

Gene3D

G3DSA:2.102.10.10; Rieske_reg; 1.

PANTHER

PTHR21266:SF2; Rng_hydr_dOase-A; 1.

Pfam

PF00355; Rieske; 1.
PF00848; Ring_hydroxyl_A; 1.
Pfam graphical view of domain structure.

PRINTS

PR00090; RNGDIOXGNASE.

PROSITE

PS51296; RIESKE; 1.
PS00570; RING_HYDROXYL_ALPHA; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q0T1Y1.

Genome annotation databases

GeneID

4207321; -.

GenomeReviews

CP000266_GR; SFV_2586.

KEGG

sfv:SFV_2586; -.

Phylogenomic databases

HOGENOM

Q0T1Y1; -.

Genome annotation databases

CMR

Q0T1Y1; SFV_2586.

Other

ProtoNet

Q0T1Y1.

UniRef

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

Keywords

2Fe-2S; Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 453`	`453`	`3-phenylpropionate/cinnamic acid dioxygenase subunit alpha.`	`PRO_0000333708`
`DOMAIN`	`44 142`	`99`	`Rieske.`
`METAL`	`85 85`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`87 87`		`Iron-sulfur (2Fe-2S) (via pros nitrogen) (By similarity).`
`METAL`	`105 105`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`108 108`		`Iron-sulfur (2Fe-2S) (via pros nitrogen) (By similarity).`
`METAL`	`213 213`		`Iron (By similarity).`
`METAL`	`218 218`		`Iron (By similarity).`

Sequence information

Length: 453 AA [This is the length of the unprocessed precursor]

Molecular weight: 51120 Da [This is the MW of the unprocessed precursor]

CRC64: 2C36276567B57045 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTPSDLNIY QLIDTQNGRV TPRIYTDPDI YQLELERIFG RCWLFLAHES QIPKPGDFFN 

        70         80         90        100        110        120 
TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNT RAFTCPYHGW SYGINGELID 

       130        140        150        160        170        180 
VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFGNWDTSA PGLHDYLGDI AWYLDGMLDR 

       190        200        210        220        230        240 
REGGTEIVGG VQKWVINCNW KFPAEQFASD QYHALFSHAS AVQVLGAKDD GSDKRLGDGQ 

       250        260        270        280        290        300 
TARPVWETAK DALQFGQDGH GSGFFFTEKP DANVWVDGAV SSYYRETYAE AEQRLGEVRA 

       310        320        330        340        350        360 
LRLAGHNNIF PTLSWLNGTA TLRVWHPRGP DQVEVWTFCI TDKAASDEVK AAFENSATRA 

       370        380        390        400        410        420 
FGPAGFLEQD DSENWCEIQK LLKGHRARNS KLCLEMGLGQ EKRRDDGIPG ITNYIFSETA 

       430        440        450 
ARGMYQRWAD LLSSESWQEV LDKTAAYQQE VMK

Q0T1Y1 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