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B7VA96 (HGD_PSEA8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:PLES_33141
OrganismPseudomonas aeruginosa (strain LESB58) [Complete proteome] [HAMAP]
Taxonomic identifier557722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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_1000119845

Sites

Active site2871Proton acceptor By similarity
Metal binding3301Iron By similarity
Metal binding3361Iron By similarity
Metal binding3661Iron By similarity
Binding site3451homogentisate By similarity
Binding site3661homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
B7VA96 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 44B17EC2A0811E2A

FASTA43247,841
        10         20         30         40         50         60 
MNLDSTALAY QSGFGNEFSS EALPGALPVG QNSPQKAPYG LYAELLSGTA FTMARSEARR 

        70         80         90        100        110        120 
TWLYRITPSA KHPPFRRLER QIAGAELDAP TPNRLRWDPL ALPEQPTDFL DGLLRMAANA 

       130        140        150        160        170        180 
PGDKPAGVSI YQYLANRSME RCFYDADGEL LLVPQLGRLR LCTELGALQV EPLEIAVIPR 

       190        200        210        220        230        240 
GMKFRVELLD GEARGYIAEN HGAPLRLPDL GPIGSNGLAN PRDFLTPVAR YEDSRQPLQL 

       250        260        270        280        290        300 
VQKYLGELWA CELDHSPLDV VAWHGNNVPY KYDLRRFNTI GTVSFDHPDP SIFTVLTSPT 

       310        320        330        340        350        360 
SVPGLANIDF VIFPPRWMVA ENTFRPPWFH RNLMNEFMGL IQGAYDAKAG GFVPGGASLH 

       370        380        390        400        410        420 
SCMSAHGPDA ESCDKAIAAD LKPHRIDQTM AFMFETSQVL RPSRAALETP ALQNDYDACW 

       430 
ASLVSTFNPQ RR 

« Hide

References

[1]"Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa."
Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.
Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LESB58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM209186 Genomic DNA. Translation: CAW28041.1.
RefSeqYP_002440900.1. NC_011770.1.

3D structure databases

ProteinModelPortalB7VA96.
SMRB7VA96. Positions 8-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557722.PLES_33141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW28041; CAW28041; PLES_33141.
GeneID7177639.
KEGGpag:PLES_33141.
PATRIC19816369. VBIPseAer113719_3415.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMARCFYNSD.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycPAER557722:GHJW-3357-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_PSEA8
AccessionPrimary (citable) accession number: B7VA96
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 39 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