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Reviewed, UniProtKB/Swiss-Prot P0ABR5 (HCAE_ECOLI)

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

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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-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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

groLP0A6F51EBI-1115311,EBI-543750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4534533-phenylpropionate/cinnamic acid dioxygenase subunit alpha HAMAP MF_01648
PRO_0000085061

Regions

Domain44 – 14299Rieske

Sites

Metal binding851Iron-sulfur (2Fe-2S) By similarity
Metal binding871Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding1051Iron-sulfur (2Fe-2S) By similarity
Metal binding1081Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding2131Iron By similarity
Metal binding2181Iron By similarity

Experimental info

Sequence conflict201V → A in CAA86018. Ref.1
Sequence conflict384 – 45370GHRAR…QEVMK → ATAPATANCVWKWGLVRKSA ATTAFLALLTISFQKLPLVE CTNAGPIF in CAA86018. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0ABR5-1 [UniParc].

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

FASTA45351,109
        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' 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. expand/collapse author list , 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.
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.

Cross-references

Sequence databases

Z37966 Genomic DNA. Translation: CAA86018.1.
U00096 Genomic DNA. Translation: AAC75591.1.
AP009048 Genomic DNA. Translation: BAA16441.1.
PIRA65031.
RefSeqAP_003124.1.
NP_417033.1.

3D structure databases

HSSPHSSP built from PDB template 1O7N based on UniProtKB P23094.
ModBaseSearch...

Protein-protein interaction databases

IntActP0ABR5. 5 interactions.

Genome annotation databases

GeneID946998.
GenomeReviewsGene locus JW2522 in contig AP009048_GR.
Gene locus b2538 in contig U00096_GR.
KEGGecj:JW2522.
eco:b2538.

Organism-specific databases

EchoBASEEB3229.
EcoGeneEG13456. hcaE.
CMRSearch...

Phylogenomic databases

HOGENOMP0ABR5.
OMAP0ABR5. LEMEFIF.

Enzyme and pathway databases

BioCycEcoCyc:PHENYLPRODIOXY-MON.
MetaCyc:PHENYLPRODIOXY-MON.

Family and domain databases

HAMAPMF_01648.
[Tree]
InterProIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
Gene3DG3DSA:2.102.10.10. Rieske_reg. 1 hit.
PANTHERPTHR21266:SF2. Rng_hydr_dOase-A. 1 hit.
PfamPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSPR00090. RNGDIOXGNASE.
PROSITEPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHCAE_ECOLI
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents