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Q5GVE9 (HGD_XANOR) 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:XOO4070
OrganismXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) [Complete proteome] [HAMAP]
Taxonomic identifier291331 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length441 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 – 441441Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_0000225798

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
Q5GVE9 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: C6C04A802F094020

FASTA44148,506
        10         20         30         40         50         60 
MHNPQHYMTG FGNEFATEAV AGSLPVGQNS PQRVAHGLYA EQLSGTAFTA PRGENRRSWL 

        70         80         90        100        110        120 
YRIRPAAVHG RFSLIEQSRL HNDFGGGPVP PDQMRWSPLP LPATPTDFVD GLYTMAGNGS 

       130        140        150        160        170        180 
PEAMTGVAVH LYAANASMHG RFFYNADGEL LLVPQLGRLR VCTELGVLEL EPQQVGVIPR 

       190        200        210        220        230        240 
GVRFRVELLD SAARGYVCEN FGGLLRLPDL GPIGANGLAN PRDFETPRAA FEQRDGAFEL 

       250        260        270        280        290        300 
VAKFQGDLWR ADIDHSPLDV VAWHGNYAPY RYDLRRFNTI GSISFDHPDP SIFTVLTSPS 

       310        320        330        340        350        360 
DTHGTANMDF AIFPPRWLVA QHTFRPPWFH RNVASEFMGL VHGVYDAKAE GFAPGGASLH 

       370        380        390        400        410        420 
NCMSGHGPDA ATFDKASQAD LTRPDVIAET MAFMFETRAV LRPTQQALSA AHRQADYQQC 

       430        440 
WSGLRAAFQH PPAKNTTSVL R 

« Hide

References

[1]"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice."
Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., Go S.-J.
Nucleic Acids Res. 33:577-586(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KACC10331 / KXO85.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013598 Genomic DNA. Translation: AAW77324.1.
RefSeqYP_202709.1. NC_006834.1.

3D structure databases

ProteinModelPortalQ5GVE9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING291331.XOO4070.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW77324; AAW77324; XOO4070.
GeneID3262364.
KEGGxoo:XOO4070.
PATRIC24107811. VBIXanOry111333_4517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMAFQSPVAC.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycXORY291331:GJBV-3764-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_XANOR
AccessionPrimary (citable) accession number: Q5GVE9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2005
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