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Q62I34 (HGD_BURMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:BMA2056
OrganismBurkholderia mallei (strain ATCC 23344) [Complete proteome] [HAMAP]
Taxonomic identifier243160 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length450 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 – 450450Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_0000225785

Sites

Active site3041Proton acceptor By similarity
Metal binding3471Iron By similarity
Metal binding3531Iron By similarity
Metal binding3831Iron By similarity
Binding site3621homogentisate By similarity
Binding site3831homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62I34 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 1BC1019C4C2C398F

FASTA45050,130
        10         20         30         40         50         60 
MERTTIMTLD FSKPGEAGYQ SGFANEFATE ALPGALPHAR NSPQRAPYGL YAEQFSGTAF 

        70         80         90        100        110        120 
TAPRGHNRRS WLYRIRPAAV HRPFELVSGE RRIVAEFGDS DDVPPTPPNQ LRWDPLPMPA 

       130        140        150        160        170        180 
QPTDFVDGWV TMAGNGSAAA MSGCAIHLYA ANRSMRERFF YSADGELLIV PQEGRLFIMT 

       190        200        210        220        230        240 
ELGRLDVEPF EIAVIPRGVR FAVALPDGRA RGYVCENFGA LLRLPDLGPI GSNGLANPRD 

       250        260        270        280        290        300 
FLTPHASYED REGAFELVAK LNGRLWRADI DHSPFDVVAW HGNYAPYKYD LRHFNTIGSI 

       310        320        330        340        350        360 
SYDHPDPSIF LVLQSQSDTP GVDAIDFVIF PPRWLAAEDT FRPPWFHRNV ASEFMGLVHG 

       370        380        390        400        410        420 
VYDAKAEGFV PGGASLHNCM SGHGPDADTF EKASSIDTSK PNKVGDTMAF MFETRTLIRP 

       430        440        450 
TRFALDTAQL QANYFECWQG LKKHFNPEQR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000010 Genomic DNA. Translation: AAU49603.1.
RefSeqYP_103636.1. NC_006348.1.

3D structure databases

ProteinModelPortalQ62I34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243160.BMA2056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU49603; AAU49603; BMA2056.
GeneID3088598.
KEGGbma:BMA2056.
PATRIC19119227. VBIBurMal55007_2124.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMARCFYNSD.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

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_BURMA
AccessionPrimary (citable) accession number: Q62I34
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 59 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