3-phenylpropionate/cinnamic acid dioxygenase subunit alpha

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P0ABR5 (HCAE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 72. History...

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

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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-phenylpropanoate + NADH + O₂ = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD⁺. HAMAP-Rule MF_01648 (2E)-3-phenylprop-2-enoate + NADH + O₂ = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD⁺. HAMAP-Rule MF_01648
Cofactor	Binds 1 2Fe-2S cluster Probable. Binds 1 iron ion Probable.
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule 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).
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NAD
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	3-phenylpropionate catabolic process Inferred from mutant phenotype PubMed 3531186 PubMed 6345502. Source: EcoCyc
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 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
Complete GO annotation...

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-Rule 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

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABR5 [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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z37966 Genomic DNA. Translation: CAA86018.1. U00096 Genomic DNA. Translation: AAC75591.1. AP009048 Genomic DNA. Translation: BAA16441.1.
PIR	A65031.
RefSeq	NP_417033.1. NC_000913.2. YP_490766.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0ABR5.
SMR	P0ABR5. Positions 9-434.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0ABR5. 5 interactions.
STRING	511145.b2538.
Proteomic databases
PRIDE	P0ABR5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75591; AAC75591; b2538. BAA16441; BAA16441; BAA16441.
GeneID	12932583. 946998.
KEGG	ecj:Y75_p2491. eco:b2538.
PATRIC	32120473. VBIEscCol129921_2639.
Organism-specific databases
EchoBASE	EB3229.
EcoGene	EG13456. hcaE.
Phylogenomic databases
eggNOG	COG4638.
HOGENOM	HOG000105925.
KO	K05708.
OMA	FRIARNM.
ProtClustDB	CLSK880425.
Enzyme and pathway databases
BioCyc	EcoCyc:PHENYLPRODIOXY-MONOMER. ECOL316407:JW2522-MONOMER. MetaCyc:PHENYLPRODIOXY-MONOMER.
UniPathway	UPA00714.
Gene expression databases
Genevestigator	P0ABR5.
Family and domain databases
Gene3D	2.102.10.10. 1 hit. 3.90.380.10. 1 hit.
HAMAP	MF_01648. HcaE.
InterPro	IPR020875. HcaE. IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C_dom. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
SUPFAM	SSF50022. Rieske_dom. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...

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:	May 29, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents