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C8U8V8 (C8U8V8_ECO10) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 35. Feed History...

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

Names and origin

Protein namesRecommended name:
3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component HAMAP-Rule MF_01651

EC=1.18.1.3 HAMAP-Rule MF_01651
Alternative name(s):
Digoxigenin system ferredoxin--NAD(+) reductase component HAMAP-Rule MF_01651
Gene names
Name:hcaD HAMAP-Rule MF_01651 EMBL BAI31817.1
Ordered Locus Names:ECO103_3062 EMBL BAI31817.1
OrganismEscherichia coli O103:H2 (strain 12009 / EHEC) [Complete proteome] [HAMAP] EMBL BAI31817.1
Taxonomic identifier585395 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_01651

Catalytic activity

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

Cofactor

FAD By similarity. HAMAP-Rule MF_01651

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) By similarity. HAMAP-Rule MF_01651

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. HAMAP-Rule MF_01651

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding5 – 3632FAD By similarity HAMAP-Rule MF_01651
Nucleotide binding146 – 17429NAD By similarity HAMAP-Rule MF_01651

Sequences

Sequence LengthMass (Da)Tools
C8U8V8 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: F5A1A7CF4F1DF2A6

FASTA40043,964
        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 LQPERSVVIV 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

[1]"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12009 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010958 Genomic DNA. Translation: BAI31817.1.
RefSeqYP_003222951.1. NC_013353.1.

3D structure databases

ProteinModelPortalC8U8V8.
SMRC8U8V8. Positions 4-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING585395.ECO103_3062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI31817; BAI31817; ECO103_3062.
GeneID8475575.
KEGGeoh:ECO103_3062.
PATRIC32098074. VBIEscCol146794_3208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycECOL585395:GJA9-3161-MONOMER.
UniPathwayUPA00714.

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...

Entry information

Entry nameC8U8V8_ECO10
AccessionPrimary (citable) accession number: C8U8V8
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: February 19, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)