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B5XQJ0 (MHPB_KLEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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
Alternative name(s):
3-carboxyethylcatechol 2,3-dioxygenase
Gene names
Name:mhpB
Ordered Locus Names:KPK_2202
OrganismKlebsiella pneumoniae (strain 342) [Complete proteome] [HAMAP]
Taxonomic identifier507522 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

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-Rule MF_01653

Catalytic activity

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

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

Cofactor

Fe2+ ion By similarity. HAMAP-Rule MF_01653

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01653

Subunit structure

Homotetramer By similarity. HAMAP-Rule 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_process3-phenylpropionate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_function3-carboxyethylcatechol 2,3-dioxygenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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-Rule MF_01653
PRO_1000187009

Sites

Active site1151Proton donor By similarity
Active site1791Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
B5XQJ0 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: A961455CEE055FD4

FASTA31434,295
        10         20         30         40         50         60 
MDAYLHCLSH TPLVGFVDPE QAVLDEVNGV IADARRRISA FEPELVVLFA PDHYNGFFYD 

        70         80         90        100        110        120 
VMPPFCLGVG ATAIGDFASA AGDLPVPTEL AEACAHAVIN SGIDLAVSYN MQVDHGFAQP 

       130        140        150        160        170        180 
LEFLLGGLDR VPVLPVFING VAAPLPGFQR TRLLGEAMGR FLNTLNKRVL ILGSGGLSHQ 

       190        200        210        220        230        240 
PPVPELAKAD AHLRDRLLGS GKQLPPDERE RRQQRVINAA RRFTEDQRSL HPLNPVWDNR 

       250        260        270        280        290        300 
FMSLLEQGRL AELDAIGNDE LSAMAGKSTH EIKTWVAAFA ALSAFGCWRS EGRYYRPIPE 

       310 
WIAGFGSLSA TTEI 

« Hide

References

[1]"Complete genome sequence of the N2-fixing broad host range endophyte Klebsiella pneumoniae 342 and virulence predictions verified in mice."
Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., Methe B.A.
PLoS Genet. 4:E1000141-E1000141(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 342.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000964 Genomic DNA. Translation: ACI06844.1.
RefSeqYP_002238038.1. NC_011283.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING507522.KPK_2202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI06844; ACI06844; KPK_2202.
GeneID6936698.
KEGGkpe:KPK_2202.
PATRIC20437860. VBIKlePne121904_2306.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG08474.
HOGENOMHOG000069851.
KOK05713.
OMAHCLSHTP.
OrthoDBEOG62ZHSQ.

Enzyme and pathway databases

BioCycKPNE507522:GI0B-2203-MONOMER.
UniPathwayUPA00714.

Family and domain databases

Gene3D3.40.830.10. 2 hits.
HAMAPMF_01653. MhpB.
InterProIPR023789. DHPP/DHXA_dioxygenase.
IPR004183. Xdiol_dOase_suB.
[Graphical view]
PfamPF02900. LigB. 1 hit.
[Graphical view]
SUPFAMSSF53213. SSF53213. 2 hits.
ProtoNetSearch...

Entry information

Entry nameMHPB_KLEP3
AccessionPrimary (citable) accession number: B5XQJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 25, 2008
Last modified: May 14, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways