3-phenylpropionate/cinnamic acid dioxygenase subunit alpha

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Q3YZ15 (HCAE_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	SSON_2620

Organism

Shigella sonnei (strain Ss046) [Complete proteome] [HAMAP]

Taxonomic identifier

300269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NAD
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3-phenylpropionate dioxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

3-phenylpropionate/cinnamic acid dioxygenase subunit alpha HAMAP MF_01648

PRO_0000333709

Regions

Domain

44 – 142

Rieske

Sites

Metal binding

Iron-sulfur (2Fe-2S) By similarity

Metal binding

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Metal binding

105

Iron-sulfur (2Fe-2S) By similarity

Metal binding

108

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Metal binding

213

Iron By similarity

Metal binding

218

Iron By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q3YZ15 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 02535BF5F47643FD
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FASTA

453

51,109

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

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

       130        140        150        160        170        180 
VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFGNWDTSA PGLRDYLGDI 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

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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.

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: AAZ89247.1.
RefSeq	YP_311482.1. NC_007384.1.
3D structure databases
HSSP	HSSP built from PDB template 2B1X based on UniProtKB Q9X3R9.
ProteinModelPortal	Q3YZ15.
SMR	Q3YZ15. Positions 5-443.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3YZ15.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000099909; EBESCP00000095938; EBESCG00000098953.
GeneID	3668240.
GenomeReviews	Gene locus SSON_2620 in contig CP000038_GR.
KEGG	ssn:SSON_2620.
PATRIC	18739629. VBIShiSon107113_3139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4638.
GeneTree	EBGT00050000010714.
HOGENOM	HBG705920.
OMA	SENWVEI.
ProtClustDB	CLSK880425.
Enzyme and pathway databases
BioCyc	SSON300269:SSO_2620-MONOMER.
Family and domain databases
HAMAP	MF_01648. HcaE. [Tree]
InterPro	IPR020875. HcaE. IPR017941. Rieske_2Fe-2S. IPR015881. Ring-hydroxy_dOase_2Fe2S_BS. IPR015879. Ring_hydroxy_dOase_asu_C. IPR001663. Rng_hydr_dOase-A. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
KO	K05708.
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
SUPFAM	SSF50022. Rieske_dom. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. PS00570. RING_HYDROXYL_ALPHA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HCAE_SHISS

Accession

Primary (citable) accession number: Q3YZ15

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 27, 2005
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents