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Q48GS7 (HGD_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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

EC=1.13.11.5
Alternative name(s):
Homogentisate oxygenase
Homogentisic acid oxidase
Homogentisicase
Gene names
Name:hmgA
Ordered Locus Names:PSPPH_3246
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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

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 – 435435Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_0000225793

Sites

Metal binding3321Iron By similarity
Metal binding3381Iron By similarity
Metal binding3681Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48GS7 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 780C40AF83FC95C0

FASTA43548,438
        10         20         30         40         50         60 
MAIHSRSDAL AYQSGFGNQF SSEALPGALP IGQNSPQKHP LGLYAEQFSG TAFTVARSEA 

        70         80         90        100        110        120 
RRTWLYRIKP SAAHPRYQRM GRQIAGQEQG PINPNRLRWN AFDIPAEPVD FIDGLIPLAS 

       130        140        150        160        170        180 
TSAADQADGV SVYVYAANTS MQRAFFSADG EWLIVPQQGR LRIITELGLL DIEPLEIAVL 

       190        200        210        220        230        240 
PRGMKFRVQL LDSSARGYIC ENHGCALRLP ELGPIGSNGL ANPRDFLTPV AWFEDNQQPV 

       250        260        270        280        290        300 
ELVQKFLGEL WSTHLEHSPF DVVGWHGNNV AYKYDLRRFN TIGTVSYDHP DPSIFTVLTS 

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

       370        380        390        400        410        420 
LHNCMSAHGP DNVTAEKAIA AELKPHKIEN TMAFMFETGK VLRPSRHALG CPQLQADYDA 

       430 
CWNDMTRTFN KEPRR 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ36498.1.
RefSeqYP_275406.1. NC_005773.3.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264730.PSPPH_3246.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ36498; AAZ36498; PSPPH_3246.
GeneID3559119.
KEGGpsp:PSPPH_3246.
PATRIC19975884. VBIPseSyr78478_3414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3508.
HOGENOMHOG000139824.
KOK00451.
OMACWEPLKS.
OrthoDBEOG6D5FZK.
ProtClustDBPRK05341.

Enzyme and pathway databases

BioCycPSAV264730:GKDE-3249-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_PSE14
AccessionPrimary (citable) accession number: Q48GS7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 54 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