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P77650 (HCAD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component

EC=1.18.1.3
Alternative name(s):
Digoxigenin system ferredoxin--NAD(+) reductase component
Gene names
Name:hcaD
Synonyms:hcaA4, phdA, yfhY
Ordered Locus Names:b2542, JW2526
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. HAMAP-Rule MF_01651

Catalytic activity

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH. HAMAP-Rule MF_01651

Cofactor

FAD.

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01651

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 ferredoxin reductase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nikRP0A6Z62EBI-1129389,EBI-562488

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4004003-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component HAMAP-Rule MF_01651
PRO_0000167661

Regions

Nucleotide binding5 – 3632FAD Potential
Nucleotide binding146 – 17429NAD Potential

Sequences

Sequence LengthMass (Da)Tools
P77650 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: F5A1A06C4F1DFF36

FASTA40043,978
        10         20         30         40         50         60 
MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS MLLEDSPQLQ 

        70         80         90        100        110        120 
QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH WDQLFIATGA AARPLPLLDA 

       130        140        150        160        170        180 
LGERCFTLRH AGDAARLREV LQPERSVVII GAGTIGLELA ASATQRRCKV TVIELAATVM 

       190        200        210        220        230        240 
GRNAPPPVQR YLLQRHQQAG VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS 

       250        260        270        280        290        300 
ANEQLAREAN LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ 

       310        320        330        340        350        360 
IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA IWFNLQNGVL 

       370        380        390        400 
IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[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] [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 277:1453-1462(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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11070 Genomic DNA. Translation: CAA71952.1.
U00096 Genomic DNA. Translation: AAC75595.1.
AP009048 Genomic DNA. Translation: BAA16445.1.
PIRE65031.
RefSeqNP_417037.1. NC_000913.3.
YP_490770.1. NC_007779.1.

3D structure databases

ProteinModelPortalP77650.
SMRP77650. Positions 5-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP77650. 7 interactions.
STRING511145.b2542.

PTM databases

PhosSiteP0809399.

Proteomic databases

PaxDbP77650.
PRIDEP77650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75595; AAC75595; b2542.
BAA16445; BAA16445; BAA16445.
GeneID12930468.
945427.
KEGGecj:Y75_p2495.
eco:b2542.
PATRIC32120481. VBIEscCol129921_2643.

Organism-specific databases

EchoBASEEB3233.
EcoGeneEG13460. hcaD.

Phylogenomic databases

eggNOGCOG0446.
HOGENOMHOG000276711.
KOK00529.
OMAHAGFQVA.
OrthoDBEOG6T4RXM.
PhylomeDBP77650.
ProtClustDBPRK09754.

Enzyme and pathway databases

BioCycEcoCyc:HCAD-MONOMER.
ECOL316407:JW2526-MONOMER.
MetaCyc:HCAD-MONOMER.
UniPathwayUPA00714.

Gene expression databases

GenevestigatorP77650.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
HAMAPMF_01651. HcaD.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR023744. HcaD.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR028202. Reductase_C.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF14759. Reductase_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
ProtoNetSearch...

Other

PROP77650.

Entry information

Entry nameHCAD_ECOLI
AccessionPrimary (citable) accession number: P77650
Secondary accession number(s): O08100
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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