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B0T816 (HGD_CAUSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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

Short name=HGDO
EC=1.13.11.5
Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase
Gene names
Name:hmgA
Ordered Locus Names:Caul_3652
OrganismCaulobacter sp. (strain K31) [Complete proteome] [HAMAP]
Taxonomic identifier366602 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length427 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 – 427427Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_1000079265

Sites

Active site2851Proton acceptor By similarity
Metal binding3281Iron By similarity
Metal binding3341Iron By similarity
Metal binding3641Iron By similarity
Binding site3431homogentisate By similarity
Binding site3641homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0T816 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 983B92E37D43B915

FASTA42746,825
        10         20         30         40         50         60 
MDLQYQSGFA NHFSTEAVPG ALPVGQNSPQ APPYGLYAEQ LSGTAFTAPR HENRRSWLYR 

        70         80         90        100        110        120 
LRPSAGHGPY APYVQERLKS GPFGAAVPTP NRLRWDPLEI PEAPLDFVDG LVTLAGNGDV 

       130        140        150        160        170        180 
ATQAGMAAHL YLANRSMIDR VFQNADGELL IVPQLGALRF VTELGVIDAA PGEVVVIPRG 

       190        200        210        220        230        240 
VRFRVELEGP VRGYVCENYG PMFRLPELGP IGSNGLANSR DFLTPVAAFE DVERPTEVIQ 

       250        260        270        280        290        300 
KFQGGLWTGT WDHSPLDVVA WHGNLAPYKY DLARFNTMGT VSFDHPDPSI FTVLTAPSEI 

       310        320        330        340        350        360 
PGTANVDFVI FPPRWMVAEH TFRPPWFHRN VMSEFMGLVT GAYDAKAGGF SPGGASLHNM 

       370        380        390        400        410        420 
MSDHGPDVAS HKAASEADLS PHKIEATMAF MFESRWVIRP TKYALETSEL QADYDACWTG 


FPKAKLP 

« Hide

References

[1]"Complete sequence of chromosome of Caulobacter sp. K31."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Stephens C., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000927 Genomic DNA. Translation: ABZ72779.1.
RefSeqYP_001685277.1. NC_010338.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING366602.Caul_3652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ72779; ABZ72779; Caul_3652.
GeneID5901107.
KEGGcak:Caul_3652.
PATRIC21320436. VBICauSp18104_4056.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMAFQSPVAC.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycCSP366602:GH0Y-3688-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_CAUSK
AccessionPrimary (citable) accession number: B0T816
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: May 14, 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