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B3QB98 (HGD_RHOPT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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

EC=1.13.11.5
Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase
Gene names
Name:hmgA
Ordered Locus Names:Rpal_5153
OrganismRhodopseudomonas palustris (strain TIE-1) [Complete proteome] [HAMAP]
Taxonomic identifier395960 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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

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_1000119850

Sites

Metal binding3461Iron By similarity
Metal binding3521Iron By similarity
Metal binding3821Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
B3QB98 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 295E932DD13B8C04

FASTA44849,832
        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 
KLTFLQGVRT MTTAGDVNTQ AGMATHLYLI TQSMVDQHFY NADGEMMFVP QQGSLRLVTE 

       190        200        210        220        230        240 
FGIITIEPAE IAVIPRGIKF 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 sequence of Rhodopseudomonas palustris TIE-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Emerson D., Newman D.K., Roden E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TIE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001096 Genomic DNA. Translation: ACF03641.1.
RefSeqYP_001994116.1. NC_011004.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395960.Rpal_5153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF03641; ACF03641; Rpal_5153.
GeneID6412853.
KEGGrpt:Rpal_5153.
PATRIC23314917. VBIRhoPal88240_5232.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMACWEPLKS.
OrthoDBEOG6D5FZK.
ProtClustDBPRK05341.

Enzyme and pathway databases

BioCycRPAL395960:GHPC-5212-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_RHOPT
AccessionPrimary (citable) accession number: B3QB98
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 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