Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B5ZZA8 (HGD_RHILW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:
Homogentisate 1,2-dioxygenase

Short name=HGDO
EC=1.13.11.5
Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase
Gene names
Name:hmgA
Ordered Locus Names:Rleg2_1407
OrganismRhizobium leguminosarum bv. trifolii (strain WSM2304) [Complete proteome] [HAMAP]
Taxonomic identifier395492 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate By similarity. HAMAP-Rule MF_00334

Catalytic activity

Homogentisate + O2 = 4-maleylacetoacetate. HAMAP-Rule MF_00334

Cofactor

Iron By similarity. HAMAP-Rule MF_00334

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6. HAMAP-Rule MF_00334

Subunit structure

Hexamer; dimer of trimers By similarity. HAMAP-Rule MF_00334

Sequence similarities

Belongs to the homogentisate dioxygenase family.

Ontologies

Keywords
   Biological processPhenylalanine catabolism
Tyrosine catabolism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processL-phenylalanine catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tyrosine catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionhomogentisate 1,2-dioxygenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_1000119849

Sites

Active site3061Proton acceptor By similarity
Metal binding3491Iron By similarity
Metal binding3551Iron By similarity
Metal binding3851Iron By similarity
Binding site3641homogentisate By similarity
Binding site3851homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
B5ZZA8 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 4E7E2BD0191D6AF4

FASTA45350,843
        10         20         30         40         50         60 
MDQTSIQASG GESATASTLK YMPGFGNDFE TESLPGALPQ GQNSPQKCNY GLYAEQLSGS 

        70         80         90        100        110        120 
PFTAPRGTNE RSWLYRIRPS VRHTRRFSNA SYPLWKTAPC LDEHSLPLGQ LRWDPIPAPE 

       130        140        150        160        170        180 
ERLTFLEGVR TITTAGDAAT QVGMSAHAYV FNQDMVDDYF FNADGELLIV PQLGALRVFT 

       190        200        210        220        230        240 
EMGIMDVEPL EICLIPRGMM FKILKTGEQA VWRGYICENY GAKFTLPDRG PIGANCLANP 

       250        260        270        280        290        300 
RDFKTPVAAF EDKETPCRVH VKWCGKFYVT EIGHSPLDVV AWHGNYAPFK YDLRTFSPVG 

       310        320        330        340        350        360 
AIRFDHPDPS IFSVLTAPTE DAGTANVDFV IFPPRWLVAE HTFRPPWYHR NIMSEFMGLI 

       370        380        390        400        410        420 
HGQYDAKEEG FVPGGMSLHN MMLPHGPDAL AFEKAANAEL KPVKLDHTMA FMFETRYPQQ 

       430        440        450 
LTKYAAELET LQDDYLECWD GLERKFDGTP GIK 

« Hide

References

[1]"Complete sequence of chromosome of Rhizobium leguminosarum bv. trifolii WSM2304."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Yates R. expand/collapse author list , Ardley J., Tiwari R.P., O'Hara G., Howieson J., Brau L., Reeve W.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM2304.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001191 Genomic DNA. Translation: ACI54701.1.
RefSeqYP_002280927.1. NC_011369.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395492.Rleg2_1407.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI54701; ACI54701; Rleg2_1407.
GeneID6980135.
KEGGrlt:Rleg2_1407.
PATRIC23126772. VBIRhiLeg95088_3219.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMARCFYNSD.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycRLEG395492:GJB3-1426-MONOMER.
UniPathwayUPA00139; UER00339.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
HAMAPMF_00334. Homogentis_dioxygen.
InterProIPR005708. Homogentis_dOase.
IPR022950. Homogentis_dOase_bac.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR11056. PTHR11056. 1 hit.
PfamPF04209. HgmA. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR01015. hmgA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHGD_RHILW
AccessionPrimary (citable) accession number: B5ZZA8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: May 14, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways