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Q4ZR64 (HGD_PSEU2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:Psyr_3326
OrganismPseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP]
Taxonomic identifier205918 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae

Protein attributes

Sequence length434 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 – 434434Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_1000019536

Sites

Active site2891Proton acceptor By similarity
Metal binding3321Iron By similarity
Metal binding3381Iron By similarity
Metal binding3681Iron By similarity
Binding site3471homogentisate By similarity
Binding site3681homogentisate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4ZR64 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: DD5AC35417020D4E

FASTA43448,391
        10         20         30         40         50         60 
MAIHSSSDAL VYQSGFGNQF SSEALPDALP VGQNSPQKHP LGLYAEQFSG TAFTVARSEA 

        70         80         90        100        110        120 
RRTWLYRIKP SAAHSRYQRM DRQMAGQEPG PINPNRLRWN AFDIPAAPTD FIDGLIPLAS 

       130        140        150        160        170        180 
TSAAEQAEGV SVYLYTANTS MQRAFFSADG EWLVVPQQGR LRIVTELGLL DIEPLEIAVL 

       190        200        210        220        230        240 
PRGLKFCVQL LDSSARGYLC ENHGCALRLP ELGPIGSNGL ANSRDFLTPV AWFEDSRQPM 

       250        260        270        280        290        300 
QLVQKFLGEL WSTQLEHSPF DVVGWHGNNV PYKYDLRRFN TIGTVSYDHP DPSIFTVLTS 

       310        320        330        340        350        360 
PGAIHGQANI DFVIFPPRWM VAENTFRPPW FHRNLMNEFM GLIDGAYDAK AEGFMPGGAS 

       370        380        390        400        410        420 
LHNCMSAHGP DNVTAEKAIA AELKPHRIDN TMAFMFETGK VLRPSRHALD CPQLQTDYDA 

       430 
CWKDMARTFT QEPR 

« Hide

References

[1]"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000."
Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E.
Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B728a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000075 Genomic DNA. Translation: AAY38358.1.
RefSeqYP_236396.1. NC_007005.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205918.Psyr_3326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY38358; AAY38358; Psyr_3326.
GeneID3368853.
KEGGpsb:Psyr_3326.
PATRIC19987294. VBIPseSyr42314_3404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMAFQSPVAC.
OrthoDBEOG6D5FZK.

Enzyme and pathway databases

BioCycPSYR205918:GJ94-3378-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_PSEU2
AccessionPrimary (citable) accession number: Q4ZR64
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 59 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