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Q2SYQ6 (HGD_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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

EC=1.13.11.5
Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase
Gene names
Name:hmgA
Ordered Locus Names:BTH_I1397
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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

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_1000019528

Sites

Metal binding3471Iron By similarity
Metal binding3531Iron By similarity
Metal binding3831Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2SYQ6 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 32406319EE771859

FASTA45050,013
        10         20         30         40         50         60 
MERTTIMTLD FSKPGEAGYQ SGFANEFATE ALPGALPHAR NSPQRAPYGL YAEQLSGTAF 

        70         80         90        100        110        120 
TAPRGHNRRS WLYRIRPAAV HRPFELVSGE RRIVADFGDS GDVPPTPPNQ 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 
FLTPNASYED 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 EKASAIDTSR PNKVGDTMAF MFETRTLIRP 

       430        440        450 
TRFALDTAQL QANYFECWQG LKKHFNPEQR 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC36904.1.
RefSeqYP_441943.1. NC_007651.1.

3D structure databases

ProteinModelPortalQ2SYQ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING271848.BTH_I1397.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC36904; ABC36904; BTH_I1397.
GeneID3846832.
KEGGbte:BTH_I1397.
PATRIC19305732. VBIBurTha36512_4174.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMACWEPLKS.
OrthoDBEOG6D5FZK.
ProtClustDBPRK05341.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-1397-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_BURTA
AccessionPrimary (citable) accession number: Q2SYQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 53 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