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Q9X4F5 (HGD_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:R02939
ORF Names:SMc03208
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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

Induction

By nitrogen and carbon deprivation as well as in the presence of tyrosine. Also induced by phenylalanine, but only in nitrogen-free medium. 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_0000220254

Sites

Active site3061Proton acceptor By similarity
Metal binding3491Iron By similarity
Metal binding3551Iron By similarity
Metal binding3851Iron By similarity
Binding site3641homogentisate By similarity
Binding site3851homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X4F5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: AC49AEFF0C783200

FASTA45350,756
        10         20         30         40         50         60 
MLEKAEKQRR AGSGQQRAAG YMPGFGNDFE TESLPGALPQ GQNSPQKCNY GLYAEQLSGS 

        70         80         90        100        110        120 
PFTAPRGTNE RSWLYRIRPS VRHTGRFRRV DYPHWKTAPH VGEHSLALGQ LRWSPLPAPS 

       130        140        150        160        170        180 
EALDFLQGIR TMTTAGDALT QAGMAAHAYA FNADMVDDYF FNADGELLIV PETGAIQVFT 

       190        200        210        220        230        240 
ELGRMDVEPS EICLIPRGMM FKVTRLGEEK VWRGYICENY GAKFTLPDRG PIGANCLANP 

       250        260        270        280        290        300 
RDFKTPVAAY EDKETPCRVQ VKWCGSFHMV EIGHSPLDVV AWHGNYAPYK YDLKTFSPVG 

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

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

       430        440        450 
LTTFAAELDT LQDDYMDCWS GLERKFDGTP GIK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel nutrient-deprivation-induced Sinorhizobium meliloti gene (hmgA) involved in the degradation of tyrosine."
Milcamps A., de Bruijn F.J.
Microbiology 145:935-947(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 1021.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF109131 Genomic DNA. Translation: AAD29874.1.
AL591688 Genomic DNA. Translation: CAC47518.1.
RefSeqNP_387045.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ9X4F5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc03208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC47518; CAC47518; SMc03208.
GeneID1234616.
KEGGsme:SMc03208.
PATRIC23635464. VBISinMel96828_4461.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMARCFYNSD.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-3008-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_RHIME
AccessionPrimary (citable) accession number: Q9X4F5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 84 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