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A6UDD3 (HGD_SINMW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:Smed_2833
OrganismSinorhizobium medicae (strain WSM419) (Ensifer medicae) [Complete proteome] [HAMAP]
Taxonomic identifier366394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length453 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 – 453453Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_1000019544

Sites

Metal binding3491Iron By similarity
Metal binding3551Iron By similarity
Metal binding3851Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A6UDD3 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 2C75617E743F9238

FASTA45350,785
        10         20         30         40         50         60 
MLEKAERQRK AAPDQQRSAG YMPGFGNDFE TESLPGSLPQ GQNSPQKCNY GLYAEQLSGS 

        70         80         90        100        110        120 
PFTAPRGTNE RSWLYRIRPS VRHTGRFTKI DYPHWKTAPH TPEHSLALGQ LRWSPLPAPS 

       130        140        150        160        170        180 
QSLTFLQGIR TMTTAGDALT QVGMAAHAYA FNADMVDDYF FNADGELLIV PETGAFQVFT 

       190        200        210        220        230        240 
ELGRIDVEPS EICLVPRGMM FKVTRLGDEK VWRGYICENY GAKFTLPDRG PIGANCLANP 

       250        260        270        280        290        300 
RDFKTPVAAY EDKETPCRVQ VKWCGSFHTA EIAHSPLDVV AWHGNYAPYK YDLKTFSPVG 

       310        320        330        340        350        360 
AILFDHPDPS IFTVLTAPSG EEGTANVDFV IFPPRWLVAE HTFRPPWYHR NIMSEFMGLI 

       370        380        390        400        410        420 
HGRYDAKEEG FVPGGMSLHN MMLAHGPDFS GFEKASNGEL KPVKLDNTMA FMFETRFPQQ 

       430        440        450 
LTTFAAELET LQDDYIDCWS GLERKFDGTP GIK 

« Hide

References

[1]"Complete sequence of Sinorhizobium medicae WSM419 chromosome."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM419.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000738 Genomic DNA. Translation: ABR61663.1.
RefSeqYP_001328498.1. NC_009636.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING366394.Smed_2833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR61663; ABR61663; Smed_2833.
GeneID5323703.
KEGGsmd:Smed_2833.
PATRIC23624831. VBISinMed134228_6043.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSMED366394:GJAL-2876-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_SINMW
AccessionPrimary (citable) accession number: A6UDD3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 44 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