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

Q7W189 (HGD_BORPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:BPP0807
OrganismBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253) [Complete proteome] [HAMAP]
Taxonomic identifier257311 [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_0000225783

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
Q7W189 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 61EC71A083C2CE66

FASTA43248,039
        10         20         30         40         50         60 
MSLQYQTGFG NACATEALPG ALPAGRNSPQ ICPYGLYAEQ LSGTAFTAPR AENRRSWLYR 

        70         80         90        100        110        120 
IRPGVQHLPF APFAGAQRWL SDFGRQPVTP NQLRWSPLPM PDAPTDFIDG MHTWGGNGGP 

       130        140        150        160        170        180 
EEQSGVGIHL YAANRSMQGR FFYNADGEML IVPQQGRLRL ATELGLIDIE PYEIAVVPRG 

       190        200        210        220        230        240 
VRLRVELLDD VARGYMLENF GTAMRLPELG PIGSNCLANA RDFQIPVAWY EDVEGDFELI 

       250        260        270        280        290        300 
AKFTGGFWRA PIAHSPLNVV AWHGTHAPYK YDLRNFNTVG SISYDHPDPS IFTVLTSPSD 

       310        320        330        340        350        360 
TPGTANMDFA IFPPRILAME NTFRPPWFHR NIASEFMGLI HGVYDAKAEG FAPGGASLHN 

       370        380        390        400        410        420 
CMSGHGPDAD TFEKASHADT SQAHYIRDTM AFMFETRRVI RPTAQALASP QRQDDYYQCW 

       430 
QGLQKHFDPE QA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640425 Genomic DNA. Translation: CAE40216.1.
RefSeqNP_883139.1. NC_002928.3.

3D structure databases

ProteinModelPortalQ7W189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257311.BPP0807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE40216; CAE40216; BPP0807.
GeneID1668662.
KEGGbpa:BPP0807.
PATRIC21145228. VBIBorPar43418_0833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMARCFYNSD.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycBPAR257311:BPP0807-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_BORPA
AccessionPrimary (citable) accession number: Q7W189
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 64 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