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A7ZI95 (MHPB_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
EC=1.13.11.16
Gene names
Name:mhpB
Ordered Locus Names:EcE24377A_0372
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively By similarity. HAMAP MF_01653

Catalytic activity

3-(2,3-dihydroxyphenyl)propanoate + O2 = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. HAMAP MF_01653

(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. HAMAP MF_01653

Cofactor

Fe2+ ion By similarity. HAMAP MF_01653

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01653

Subunit structure

Homotetramer By similarity. HAMAP MF_01653

Sequence similarities

Belongs to the ligB/mhpB extradiol dioxygenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandIron
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-carboxyethylcatechol 2,3-dioxygenase activity

Inferred from electronic annotation. Source: EC

ferrous iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3143142,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP MF_01653
PRO_0000337650

Sites

Active site1151Proton donor By similarity
Active site1791Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZI95 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 8AA5A8574E5DEA54

FASTA31434,226
        10         20         30         40         50         60 
MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD 

        70         80         90        100        110        120 
VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP 

       130        140        150        160        170        180 
LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ 

       190        200        210        220        230        240 
PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ 

       250        260        270        280        290        300 
FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISTFGNWRS EGRYYRPIPE 

       310 
WIAGFGSLSA RTEN

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000800 Genomic DNA. Translation: ABV19400.1.
RefSeqYP_001461524.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZI95.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZI95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000020664; EBESCP00000019726; EBESCG00000019718.
GeneID5589309.
GenomeReviewsGene locus EcE24377A_0372 in contig CP000800_GR.
KEGGecw:EcE24377A_0372.
PATRIC18290012. VBIEscCol31211_0686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG42398.
GeneTreeEBGT00050000010475.
HOGENOMHBG565586.
OMAAHEIRTW.
ProtClustDBPRK13370.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_0372-MONOMER.

Family and domain databases

HAMAPMF_01653. MhpB.
[Tree]
InterProIPR023789. DHPP/DHXA_dioxygenase.
IPR004183. Xdiol_dOase_suB.
[Graphical view]
Gene3DG3DSA:3.40.830.10. Xdiol_dOase_3B. 2 hits.
KOK05713.
PfamPF02900. LigB. 1 hit.
[Graphical view]
SUPFAMSSF53213. Xdiol_dOase_3B. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMHPB_ECO24
AccessionPrimary (citable) accession number: A7ZI95
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 31 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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