[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Turlin E., Gasser F., Biville F.; Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[2]	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).
[3]	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).
[4]	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).
[5]	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⁺.
COFACTOR: Binds 1 2Fe-2S cluster (Probable).
COFACTOR: Binds 1 iron ion (Probable).
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).
INTERACTION:
P0A6F5:groL; NbExp=1; IntAct=EBI-1115311, EBI-543750;
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

Z37966; CAA86018.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75591.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16441.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A65031; A65031.

RefSeq

AP_003124.1; -.
NP_417033.1; -.

3D structure databases

HSSP

P23094; 1O7N. [HSSP ENTRY / PDB]

ModBase

P0ABR5.

Protein-protein interaction databases

IntAct

P0ABR5; -.

Enzyme and pathway databases

BioCyc

EcoCyc:PHENYLPRODIOXY-MON; -.
MetaCyc:PHENYLPRODIOXY-MON; -.

Organism-specific databases

EchoBASE

EB3229; -.

EcoGene

EG13456; hcaE.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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

P0ABR5.

Genome annotation databases

GeneID

946998; -.

GenomeReviews

U00096_GR; b2538.
AP009048_GR; JW2522.

KEGG

ecj:JW2522; -.
eco:b2538; -.

Phylogenomic databases

HOGENOM

P0ABR5; -.

Genome annotation databases

CMR

P0ABR5; b2538.

Other

ProtoNet

P0ABR5.

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_0000085061`
`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).`
`CONFLICT`	`20 20`		`V -> A (in Ref. 1; CAA86018).`
`CONFLICT`	`384 453`		`GHRARNSKLCLEMGLGQEKRRDDGIPGITNYIFSETAARG` `MYQRWADLLSSESWQEVLDKTAAYQQEVMK -> ATAPATANCVWKWGLVRKSAATTAFLALLTISFQKLPLVE` `CTNAGPIF (in Ref. 1; CAA86018).`

Sequence information

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

Molecular weight: 51109 Da [This is the MW of the unprocessed precursor]

CRC64: 02535BF5F47643FD [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 PGLRDYLGDI 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 DQVEVWAFCI TDKAASDEVK AAFENSATRA 

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

       430        440        450 
ARGMYQRWAD LLSSESWQEV LDKTAAYQQE VMK

P0ABR5 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