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Q0K0L8 (HGD_CUPNH) 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:H16_B1671
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length439 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 – 439439Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_1000019537

Sites

Active site2931Proton acceptor By similarity
Metal binding3361Iron By similarity
Metal binding3421Iron By similarity
Metal binding3721Iron By similarity
Binding site3511homogentisate By similarity
Binding site3721homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0K0L8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 29652C9DEC46E3A0

FASTA43948,708
        10         20         30         40         50         60 
MTLTHTQLAE HGYMSGFANE FATEALPGAL PVGRNSPQCA PYGLYAEQLS GTAFTAPRAH 

        70         80         90        100        110        120 
NRRSWLYRIR PAAMHTPFTQ IEQSRFLSRF DQVPPSPNQM RWSPPAMPSV PTDFVDGIVT 

       130        140        150        160        170        180 
MAGNGGPEAM TGCGIHLYLA NQSMQDRFFY NADGEMLIVP QQGRLLMVTE LGRLEVEPQE 

       190        200        210        220        230        240 
IVVIPRGVRF RVELPDGEAR GYICENYGAL FQLPDLGVIG SNGLANPRDF LSPVASYEDR 

       250        260        270        280        290        300 
EGDFELVAKF QGNLWRAGIG HSPLDVVAWH GNYTPYKYDL RRFNTIGSIS FDHPDPSIFL 

       310        320        330        340        350        360 
VLQSPSATPG VDTIDFVIFG PRWLAMQDSF RPPWFHRNIA SEFMGLITGV YDAKAEGFAP 

       370        380        390        400        410        420 
GGASLHNCMS GHGPDAETFE KASAADTSKP HRIEDTMAFM FETPGVIRPT PYAAQSASLQ 

       430 
QDYYTCWQGL KKHFNPNTR 

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260480 Genomic DNA. Translation: CAJ96456.1.
RefSeqYP_841186.1. NC_008314.1.

3D structure databases

ProteinModelPortalQ0K0L8.
SMRQ0K0L8. Positions 9-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_B1671.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ96456; CAJ96456; H16_B1671.
GeneID4455534.
KEGGreh:H16_B1671.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMAFQSPVAC.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-5374-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_CUPNH
AccessionPrimary (citable) accession number: Q0K0L8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 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