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Q83K39 (HCAE_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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 alpha
EC=1.14.12.19
Alternative name(s):
Digoxigenin subunit alpha
Gene names
Name:hcaE
Ordered Locus Names:SF2585, S2757
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length453 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_01648

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+.

Cofactor

Binds 1 iron ion By similarity. HAMAP MF_01648

Binds 1 2Fe-2S cluster per subunit By similarity. HAMAP MF_01648

Pathway

Aromatic compound metabolism; 3-phenylpropanoate 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) By similarity.

Sequence similarities

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

Contains 1 Rieske domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4534533-phenylpropionate/cinnamic acid dioxygenase subunit alpha HAMAP MF_01648
PRO_0000333707

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

Sequences

Sequence LengthMass (Da)Tools
Q83K39 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: C1EB5F940708316C

FASTA45351,076
        10         20         30         40         50         60 
MTTPSDLNIY QLIDTQNGRV TPRIYTDPDI YQLELERIFG RCWLFLAHES QIPKPGDFFN 

        70         80         90        100        110        120 
TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNS RAFTCPYHGW SYGINGELID 

       130        140        150        160        170        180 
VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFGNWDTSA PGLHDYLGDI 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

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005674 Genomic DNA. Translation: AAN44084.1.
AE014073 Genomic DNA. Translation: AAP17909.1.
RefSeqNP_708377.1. NC_004337.2.
NP_838099.1. NC_004741.1.

3D structure databases

HSSPHSSP built from PDB template 2B1X based on UniProtKB Q9X3R9.
ProteinModelPortalQ83K39.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000088148; EBESCP00000084970; EBESCG00000087193.
EBESCT00000089660; EBESCP00000086296; EBESCG00000088704.
GeneID1026946.
1078029.
GenomeReviewsGene locus SF2585 in contig AE005674_GR.
Gene locus S2757 in contig AE014073_GR.
KEGGsfl:SF2585.
sfx:S2757.
PATRIC18707146. VBIShiFle31049_3041.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010714.
HOGENOMHBG705920.
OMASENWVEI.
ProtClustDBCLSK880425.

Enzyme and pathway databases

BioCycSFLE198214:AAN44084.1-MONOMER.

Family and domain databases

HAMAPMF_01648. HcaE.
[Tree]
InterProIPR020875. HcaE.
IPR017941. 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.
KOK05708.
PfamPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSPR00090. RNGDIOXGNASE.
SUPFAMSSF50022. Rieske_dom. 1 hit.
PROSITEPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHCAE_SHIFL
AccessionPrimary (citable) accession number: Q83K39
Secondary accession number(s): Q7C0G4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 68 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

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