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Q6N0T9 (HGD_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. 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:RPA4672
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length448 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 – 448448Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_0000225795

Sites

Active site3031Proton acceptor By similarity
Metal binding3461Iron By similarity
Metal binding3521Iron By similarity
Metal binding3821Iron By similarity
Binding site3611homogentisate By similarity
Binding site3821homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6N0T9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 1E3C3C8BB33EE45D

FASTA44849,761
        10         20         30         40         50         60 
MNINAAPQIL GRSSQDITPG YMSGFGNSFE TEALPGALPV GRNSPQRCAY GLYAEQLSGS 

        70         80         90        100        110        120 
PFTAPRGANE RSWLYRIRPS VKHSGRFAKT DMGLWRSAPC FEHDLPIAQL RWDPPPMPQE 

       130        140        150        160        170        180 
ALTFLQGVRT MTTAGDVNTQ AGMATHLYLI TQSMVDQHFY NADGEMMFVP QQGSLRLVTE 

       190        200        210        220        230        240 
FGIITIEPAE IAVIPRGVKF RVELVDGPAR GYLCENYGGA FTLPERGPIG ANCLANSRDF 

       250        260        270        280        290        300 
LTPVAAYEDK DTPTELYVKW GGSLYVTKLP HSPIDVVAWH GNYAPYKYDL RTYSPVGAIG 

       310        320        330        340        350        360 
FDHPDPSIFT VLTSPSETPG TANIDFVIFP ERWMVADNTF RPPWYHMNIM SEFMGLIYGV 

       370        380        390        400        410        420 
YDAKPQGFVP GGASLHNMML PHGPDREAFD HASNGELKPV KLTGTMAFMF ETRYPQRVTE 

       430        440 
YAASSGLLQD DYADCWNGLE KRFDPNRP 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572608 Genomic DNA. Translation: CAE30112.1.
RefSeqNP_950006.1. NC_005296.1.

3D structure databases

ProteinModelPortalQ6N0T9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING258594.RPA4672.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE30112; CAE30112; RPA4672.
GeneID2692302.
KEGGrpa:RPA4672.
PATRIC23294017. VBIRhoPal84835_4909.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMAFQSPVAC.
OrthoDBEOG6D5FZK.
PhylomeDBQ6N0T9.

Enzyme and pathway databases

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_RHOPA
AccessionPrimary (citable) accession number: Q6N0T9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 63 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