3-phenylpropionate/cinnamic acid dioxygenase subunit alpha

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Reviewed, UniProtKB/Swiss-Prot P0ABR5 (HCAE_ECOLI)

Last modified June 16, 2009. Version 35. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    3-phenylpropionate/cinnamic acid dioxygenase subunit alpha
    EC=1.14.12.19
Alternative name(s):
    Digoxigenin subunit alpha

Gene names

Name:	hcaE
Synonyms:	digA, hcaA, hcaA1, phdC1, yfhU
Ordered Locus Names:	b2538, JW2522

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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_01648 Cinnamic acid + H⁺ + NADH + O₂ = cis-3-(2-carboxyethenyl)-3,5-cyclohexadiene-1,2-diol + NAD⁺. HAMAP MF_01648
Cofactor	Binds 1 2Fe-2S cluster Probable. Binds 1 iron ion Probable.
Pathway	Aromatic compound metabolism; 3-phenylpropionic acid degradation. HAMAP MF_01648
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_01648
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain.

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Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding 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	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: HAMAP electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding 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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1115311,EBI-543750

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

3-phenylpropionate/cinnamic acid dioxygenase subunit alpha HAMAP MF_01648

PRO_0000085061

Regions

Domain

44 – 142

Rieske

Sites

Metal binding

Iron-sulfur (2Fe-2S) By similarity

Metal binding

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Metal binding

105

Iron-sulfur (2Fe-2S) By similarity

Metal binding

108

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Metal binding

213

Iron By similarity

Metal binding

218

Iron By similarity

Experimental info

Sequence conflict

V → A in CAA86018. Ref.1

Sequence conflict

384 – 453

GHRAR…QEVMK → ATAPATANCVWKWGLVRKSA ATTAFLALLTISFQKLPLVE CTNAGPIF in CAA86018. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P0ABR5-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 02535BF5F47643FD
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FASTA

453

51,109

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Turlin E., Gasser F., Biville F. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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. 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.
[3]	"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.
[4]	"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.
[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: FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

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Cross-references

Sequence databases
	Z37966 Genomic DNA. Translation: CAA86018.1. U00096 Genomic DNA. Translation: AAC75591.1. AP009048 Genomic DNA. Translation: BAA16441.1.
PIR	A65031.
RefSeq	AP_003124.1. NP_417033.1.
3D structure databases
HSSP	HSSP built from PDB template 1O7N based on UniProtKB P23094.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0ABR5. 5 interactions.
Genome annotation databases
GeneID	946998.
GenomeReviews	Gene locus JW2522 in contig AP009048_GR. Gene locus b2538 in contig U00096_GR.
KEGG	ecj:JW2522. eco:b2538.
Organism-specific databases
EchoBASE	EB3229.
EcoGene	EG13456. hcaE.
CMR	Search...
Phylogenomic databases
HOGENOM	P0ABR5.
OMA	P0ABR5. LEMEFIF.
Enzyme and pathway databases
BioCyc	EcoCyc:PHENYLPRODIOXY-MON. MetaCyc:PHENYLPRODIOXY-MON.
Family and domain databases
HAMAP	MF_01648. [Tree]
InterPro	IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
PANTHER	PTHR21266:SF2. Rng_hydr_dOase-A. 1 hit.
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
PROSITE	PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HCAE_ECOLI

Accession

Primary (citable) accession number: P0ABR5
Secondary accession number(s): P77590, P78203, Q47139

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents