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Q07T66 (HGD_RHOP5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:RPE_0912
OrganismRhodopseudomonas palustris (strain BisA53) [Complete proteome] [HAMAP]
Taxonomic identifier316055 [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_1000019541

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
Q07T66 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 8AD41FEE444CD97C

FASTA44849,438
        10         20         30         40         50         60 
MNINTVPELI GRGSASITPG YMSGFKNSFE TEALPGALPI GRNSPQRCAY GLYAEQLSGS 

        70         80         90        100        110        120 
PFTAPRGSNE RSWLYRIRPS VKHSGRFAKA DVGLWRTAPC HEHEMPIAQL RWDPPPLPQH 

       130        140        150        160        170        180 
EQTFLQGVVT MTTAGDANTQ AGMAAHIYLI TASMVDQAFY NADGELMFVP QQGSLRFVTE 

       190        200        210        220        230        240 
FGRIDAGPGE IVVIPRGVKF RVELTGGPAR GYLCENYGGA FTLPERGPIG ANCLANARDF 

       250        260        270        280        290        300 
LTPVAAYEDK DTPTELFVKW GGTLWATTLP YSPIDVVAWH GNYAPYKYDL RTFSPVGAIG 

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

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

       430        440 
YAATSGLLQP DYADCWTGLE KRFDPTRP 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisA53."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisA53.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000463 Genomic DNA. Translation: ABJ04868.1.
RefSeqYP_779848.1. NC_008435.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316055.RPE_0912.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ04868; ABJ04868; RPE_0912.
GeneID4357772.
KEGGrpe:RPE_0912.
PATRIC23256360. VBIRhoPal93214_0933.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMATTETHKL.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycRPAL316055:GHR9-927-MONOMER.
UniPathwayUPA00139; UER00339.

Family and domain databases

Gene3D2.60.120.10. 3 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_RHOP5
AccessionPrimary (citable) accession number: Q07T66
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 31, 2006
Last modified: May 14, 2014
This is version 51 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