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Protein

3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component

Gene

hcaD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

Pathway: 3-phenylpropanoate degradation

This protein is involved in the pathway 3-phenylpropanoate degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway 3-phenylpropanoate degradation and in Aromatic compound metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi5 – 3632FADSequence AnalysisAdd
BLAST
Nucleotide bindingi146 – 17429NADSequence AnalysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • 3-phenylpropionate catabolic process Source: EcoCyc
  • cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciEcoCyc:HCAD-MONOMER.
ECOL316407:JW2526-MONOMER.
MetaCyc:HCAD-MONOMER.
UniPathwayiUPA00714.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component (EC:1.18.1.3)
Gene namesi
Name:hcaD
Synonyms:hcaA4, phdA, yfhY
Ordered Locus Names:b2542, JW2526
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13460. hcaD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4004003-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase componentPRO_0000167661Add
BLAST

Proteomic databases

PaxDbiP77650.
PRIDEiP77650.

Interactioni

Subunit structurei

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
nikRP0A6Z62EBI-1129389,EBI-562488

Protein-protein interaction databases

IntActiP77650. 7 interactions.
STRINGi511145.b2542.

Structurei

3D structure databases

ProteinModelPortaliP77650.
SMRiP77650. Positions 5-386.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0446.
HOGENOMiHOG000276711.
InParanoidiP77650.
KOiK00529.
OMAiHAGFQVA.
OrthoDBiEOG6T4RXM.
PhylomeDBiP77650.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
HAMAPiMF_01651. HcaD.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF14759. Reductase_C. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

P77650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS
60 70 80 90 100
MLLEDSPQLQ QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH
110 120 130 140 150
WDQLFIATGA AARPLPLLDA LGERCFTLRH AGDAARLREV LQPERSVVII
160 170 180 190 200
GAGTIGLELA ASATQRRCKV TVIELAATVM GRNAPPPVQR YLLQRHQQAG
210 220 230 240 250
VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS ANEQLAREAN
260 270 280 290 300
LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ
310 320 330 340 350
IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA
360 370 380 390 400
IWFNLQNGVL IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL
Length:400
Mass (Da):43,978
Last modified:February 1, 1997 - v1
Checksum:iF5A1A06C4F1DFF36
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11070 Genomic DNA. Translation: CAA71952.1.
U00096 Genomic DNA. Translation: AAC75595.1.
AP009048 Genomic DNA. Translation: BAA16445.1.
PIRiE65031.
RefSeqiNP_417037.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75595; AAC75595; b2542.
BAA16445; BAA16445; BAA16445.
GeneIDi945427.
KEGGiecj:Y75_p2495.
eco:b2542.
PATRICi32120481. VBIEscCol129921_2643.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11070 Genomic DNA. Translation: CAA71952.1.
U00096 Genomic DNA. Translation: AAC75595.1.
AP009048 Genomic DNA. Translation: BAA16445.1.
PIRiE65031.
RefSeqiNP_417037.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP77650.
SMRiP77650. Positions 5-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP77650. 7 interactions.
STRINGi511145.b2542.

Proteomic databases

PaxDbiP77650.
PRIDEiP77650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75595; AAC75595; b2542.
BAA16445; BAA16445; BAA16445.
GeneIDi945427.
KEGGiecj:Y75_p2495.
eco:b2542.
PATRICi32120481. VBIEscCol129921_2643.

Organism-specific databases

EchoBASEiEB3233.
EcoGeneiEG13460. hcaD.

Phylogenomic databases

eggNOGiCOG0446.
HOGENOMiHOG000276711.
InParanoidiP77650.
KOiK00529.
OMAiHAGFQVA.
OrthoDBiEOG6T4RXM.
PhylomeDBiP77650.

Enzyme and pathway databases

UniPathwayiUPA00714.
BioCyciEcoCyc:HCAD-MONOMER.
ECOL316407:JW2526-MONOMER.
MetaCyc:HCAD-MONOMER.

Miscellaneous databases

PROiP77650.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
HAMAPiMF_01651. HcaD.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF14759. Reductase_C. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiHCAD_ECOLI
AccessioniPrimary (citable) accession number: P77650
Secondary accession number(s): O08100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.