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Q9F9U5 (MHPB2_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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 2
EC=1.13.11.16
Gene names
Name:mhpB2
Synonyms:cbzE2
Encoded onPlasmid pHMT112 Ref.1
Plasmid pKW1 Ref.2
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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.

Sequence caution

The sequence AAX50134.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandIron
   Molecular functionDioxygenase
Oxidoreductase
   Technical termPlasmid
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 2 HAMAP MF_01653
PRO_0000337663

Sites

Active site1151Proton donor By similarity
Active site1791Proton acceptor By similarity

Experimental info

Sequence conflict201N → T in AAX50134. Ref.1
Sequence conflict701E → A in AAX50134. Ref.1
Sequence conflict811A → V in AAX50134. Ref.1
Sequence conflict89 – 902DV → EL in AAX50134. Ref.1
Sequence conflict1221D → E in AAX50134. Ref.1
Sequence conflict1561D → E in AAX50134. Ref.1
Sequence conflict2031N → D in AAX50134. Ref.1
Sequence conflict2151R → Q in AAX50134. Ref.1
Sequence conflict2261N → D in AAX50134. Ref.1
Sequence conflict2391R → Q in AAX50134. Ref.1
Sequence conflict2501L → V in AAX50134. Ref.1
Sequence conflict2591A → S in AAX50134. Ref.1
Sequence conflict2831S → A in AAX50134. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9F9U5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F1B8670FF5D5BD50

FASTA31434,581
        10         20         30         40         50         60 
MNAYLHCLSH TPLIGHFDPN QDVLDEVAEV VRAARARIEA FNPELVVLFA PDHYNGFFYD 

        70         80         90        100        110        120 
VMPPFCLGME AEAIGDFGSL AGTLSVPKDV AEACAESVLT SGIDLAVSYR MQVDHGFAQP 

       130        140        150        160        170        180 
LDFLLGGLDK YPVLPVFVNC VAPPLPTFER VRLLGDAIGR FTRGLNKRVL FLGSGGLSHQ 

       190        200        210        220        230        240 
PPVPELAKVD ARMADRLMGS GRNLPPEERD ARTQRVVVAA ERFVENQNTL HPLNPKWDRY 

       250        260        270        280        290        300 
FLDVVEQDLL SQLDDLSNAH LSELAGKSTH EVKAWVAAFS ALSAHGAYTA TDRYYRPIPE 

       310 
WIAGFGSISA HTQR

« Hide

References

[1]"mhpB from Pseudomonas putida ML2."
Panicker G., Tan H.M.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ML2.
[2]"GJ31 meta-operon."
Reineke W., Kunze M.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GJ31.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF176355 Genomic DNA. Translation: AAG09232.1.
AY831461 Genomic DNA. Translation: AAX50134.1. Different initiation.

3D structure databases

ProteinModelPortalQ9F9U5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
PfamPF02900. LigB. 1 hit.
[Graphical view]
SUPFAMSSF53213. Xdiol_dOase_3B. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMHPB2_PSEPU
AccessionPrimary (citable) accession number: Q9F9U5
Secondary accession number(s): Q49KF7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 38 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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