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Q5X5S2 (HGD_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:lpp1248
OrganismLegionella pneumophila (strain Paris) [Complete proteome] [HAMAP]
Taxonomic identifier297246 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length416 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 – 416416Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_0000225790

Sites

Active site2751Proton acceptor By similarity
Metal binding3181Iron By similarity
Metal binding3241Iron By similarity
Metal binding3541Iron By similarity
Binding site3331homogentisate By similarity
Binding site3541homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5X5S2 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 2A4D511B622A974D

FASTA41647,433
        10         20         30         40         50         60 
MYLQGFGNYH HSEAVKGALP TNQNSPQHCS LGLYAEQLSG TSFTRPRHNN LRSWLYRILP 

        70         80         90        100        110        120 
TVTQGTYYPY EFNVMQPFVD ELSPNAMRWS PLYNSSQIKC DFVEGLFHIA GSPLVNTYTY 

       130        140        150        160        170        180 
YCNHSMSDKY FANNDGELLF VPYAGEIHLH TEFGKLILSS GSIAVIPRGV KFKVEVISKE 

       190        200        210        220        230        240 
AKGYLCENSG NPLTLPQLGP IGANGLANPR HFQYPVAAFE NSGGEHTIIC KNQKKLWFTV 

       250        260        270        280        290        300 
CNHSPLNVVA WHGNYAPYCY DLSLFNTINT VSFDHPDPSI FTVLTSESEI PGVSNLDFVI 

       310        320        330        340        350        360 
FPPRWMVAEH TFRPPYFHRN YMNELMGLVY GEYDAKKEGF IPGGISIHNC MTPHGPDYES 

       370        380        390        400        410 
YEIAASQDLK PNYINSLAFM FETKDYWQVT EQAYRHPSRQ MDYLNCWQGF KIEFSQ 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628336 Genomic DNA. Translation: CAH12399.1.
RefSeqYP_123572.1. NC_006368.1.

3D structure databases

ProteinModelPortalQ5X5S2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297246.lpp1248.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH12399; CAH12399; lpp1248.
GeneID3117133.
KEGGlpp:lpp1248.
PATRIC22322849. VBILegPne27771_1484.

Organism-specific databases

LegioListlpp1248.
CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMARCFYNSD.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycLPNE297246:GCO9-1598-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_LEGPA
AccessionPrimary (citable) accession number: Q5X5S2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 62 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