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Q3YZ14 (HCAF_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-phenylpropionate/cinnamic acid dioxygenase subunit beta

EC=1.14.12.19
Alternative name(s):
Digoxigenin subunit beta
Gene names
Name:hcaF
Ordered Locus Names:SSON_2621
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_01649

Catalytic activity

3-phenylpropanoate + NADH + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+.

(2E)-3-phenylprop-2-enoate + NADH + O2 = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NAD+.

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01649

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.

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1721723-phenylpropionate/cinnamic acid dioxygenase subunit beta HAMAP MF_01649
PRO_0000333717

Sequences

Sequence LengthMass (Da)Tools
Q3YZ14 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 8958F95B6FF9E0D0

FASTA17220,636
        10         20         30         40         50         60 
MSAQVSLELH HRISQFLFHE ASLLDDWKFR DWLEQLDKEI RYTMRTTVNA QTRDRRKGVQ 

        70         80         90        100        110        120 
PPTTWIFNDT KDQLERRIAR LETGMAWAEE PPSRTRHLIS NCQISETDIP NVFAVRVNYL 

       130        140        150        160        170 
LYRAQKERDE TFYVGTRFDK VRRLEDDNWR LLERDIVLDQ AVITSHNLSV LF 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000038 Genomic DNA. Translation: AAZ89248.1.
RefSeqYP_311483.1. NC_007384.1.

3D structure databases

HSSPHSSP built from PDB template 2B1X based on UniProtKB Q9WVZ0.
ProteinModelPortalQ3YZ14.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3YZ14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000099508; EBESCP00000095537; EBESCG00000098552.
GeneID3668241.
GenomeReviewsGene locus SSON_2621 in contig CP000038_GR.
KEGGssn:SSON_2621.
PATRIC18739631. VBIShiSon107113_3140.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5517.
GeneTreeEBGT00050000011518.
HOGENOMHBG582498.
OMADIFAGER.
ProtClustDBPRK10069.

Enzyme and pathway databases

BioCycSSON300269:SSO_2621-MONOMER.

Family and domain databases

HAMAPMF_01649. HcaF.
[Tree]
InterProIPR023712. HcaF.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
KOK05709.
PfamPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHCAF_SHISS
AccessionPrimary (citable) accession number: Q3YZ14
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 27, 2005
Last modified: January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families