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Q2KYC8 (HGD_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:BAV0528
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length432 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 – 432432Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_1000019520

Sites

Active site2861Proton acceptor By similarity
Metal binding3291Iron By similarity
Metal binding3351Iron By similarity
Metal binding3651Iron By similarity
Binding site3441homogentisate By similarity
Binding site3651homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KYC8 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 2CEC82ACE2DE950E

FASTA43247,808
        10         20         30         40         50         60 
MPLNYQSGFG NACATEALPG ALPQGRNSPQ QCPYGLYAEQ LSGTAFTAPR SENRRSWLYR 

        70         80         90        100        110        120 
IRPGVVHRPF EPYAGAPHWL ADFGTGPVTP NQLRWSPLPL PATPTDFIDG VHTWGGNGGP 

       130        140        150        160        170        180 
DEQSGVGIHL YAANQSMKGR FFYNADAEML LVPQLGRLRL ATEMGLLDLE PLEIAVLPRG 

       190        200        210        220        230        240 
VRFRVELLDA EARGYLLENF GTALRPPELG PIGSNGLANA RDFQTPVAWY EDVEGDFELI 

       250        260        270        280        290        300 
AKFTGGFWRA PLTHSPLDVV AWHGTHAPYK YDLRHFNTIG SISYDHPDPS IFTVLTSPSD 

       310        320        330        340        350        360 
TPGTANLDFA IFPPRILAME NTFRPPWFHR NIASEFMGLI QGVYDAKAEG FAPGGASLHN 

       370        380        390        400        410        420 
CMSGHGPDAD TFEKASVADT SKAHYIRDTM AFMFETRRVI RPTRQALASA QLQGDYYQCW 

       430 
QDLKKHFNPE KA 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ48133.1.
RefSeqYP_785061.1. NC_010645.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV0528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6266951.
KEGGbav:BAV0528.
PATRIC21127210. VBIBorAvi43433_0541.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMATTETHKL.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycBAVI360910:GCKI-538-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_BORA1
AccessionPrimary (citable) accession number: Q2KYC8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 54 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