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A0PL52 (MHPB_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:
2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
EC=1.13.11.16
Gene names
Name:mhpB
Ordered Locus Names:MUL_0347
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length313 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.

Sequence caution

The sequence ABL03071.1 differs from that shown. Reason: Erroneous initiation.

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 – 3133132,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP MF_01653
PRO_0000337659

Sites

Active site1151Proton donor By similarity
Active site1791Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PL52 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 0EB633671CBFC800

FASTA31333,564
        10         20         30         40         50         60 
MALALCRMSH SPLLNLPGPR LDLLDEVHAA IAEAAEFVRA YDPDLVVIFS PDHYNGFFYR 

        70         80         90        100        110        120 
AMHPFCIGMY ASAVGDYGTH IGALDVPTDL AADCAKAVLG ADVDVAVSAS MDVDHGTVQP 

       130        140        150        160        170        180 
LEKLFGTATA RPVIPIFINA IAAPLGPLRR CRALGTAVGT FLSTLDLRVL VIGSGGLSHS 

       190        200        210        220        230        240 
PPVPTLHSAD PQVRERIVHG QPLTPAQRQA RQTVVMEAAK SFAAGNSDLQ PLNPAWDQRF 

       250        260        270        280        290        300 
LEIIDNGHLS DLDRWSNSFV THEGGSLAHE IRTWISAFAA MAVAGPYQTK VRYYKQAADL 

       310 
IAGFAIRTAV PIP

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References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000325 Genomic DNA. Translation: ABL03071.1. Different initiation.
RefSeqYP_904542.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PL52.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PL52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000073733; EBMYCP00000071738; EBMYCG00000073728.
GeneID4550878.
GenomeReviewsGene locus MUL_0347 in contig CP000325_GR.
KEGGmul:MUL_0347.
PATRIC18167198. VBIMycUlc37413_0477.

Organism-specific databases

GenoListMUL_0347.
CMRSearch...

Phylogenomic databases

eggNOGNOG42398.
GeneTreeEBGT00050000017557.
HOGENOMHBG565586.
ProtClustDBPRK13370.

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_MYCUA
AccessionPrimary (citable) accession number: A0PL52
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 36 of the entry and version 2 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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