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Q4UZI9 (HGD_XANC8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:XC_0452
OrganismXanthomonas campestris pv. campestris (strain 8004) [Complete proteome] [HAMAP]
Taxonomic identifier314565 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length455 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 – 455455Homogentisate 1,2-dioxygenase HAMAP-Rule MF_00334
PRO_0000225796

Sites

Metal binding3511Iron By similarity
Metal binding3571Iron By similarity
Metal binding3871Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4UZI9 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 2225A12DAD492A23

FASTA45550,406
        10         20         30         40         50         60 
MIQLDPTLLL SWRAGQHPDA PMHNDQRYMT GFGNEFASEA VADTLPVGQN SPQRVAHGLY 

        70         80         90        100        110        120 
AEQLSGTAFT APRGENRRSW LYRMRPAAVH GTFSLIEQSQ FHNDFGHGPV PPDQLRWSPL 

       130        140        150        160        170        180 
PLPQTPTDFI DGLYTMAGNG SPEAMNGVAV HLYAANASMQ DRFFYNADGE LLLVPQLGRL 

       190        200        210        220        230        240 
RVHTELGMLE LEPQQIGVIP RGVRFRVELR DGTARGYVCE NFGGLLHLPD LGPIGSNGLA 

       250        260        270        280        290        300 
NPRDFETPCA AFEQREGRFE LVAKFQGHLW RADIGHSPLD VVAWHGNYAP YRYDLRRFNT 

       310        320        330        340        350        360 
IGSISFDHPD PSIFTVLTSP SDTHGTANMD FAIFPPRWLV AQHTFRPPWF HRNVASEFMG 

       370        380        390        400        410        420 
LVHGVYDAKA DGFAPGGASL HNCMSGHGPD AATFDKASQA DLSRPDVITE TMAFMFETRA 

       430        440        450 
VLRPTAQALH APHRQGDYQQ CWAGLRKAFQ APPAS 

« Hide

References

[1]"Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris."
Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L. expand/collapse author list , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.
Genome Res. 15:757-767(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 8004.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000050 Genomic DNA. Translation: AAY47534.1.
RefSeqYP_241554.1. NC_007086.1.

3D structure databases

ProteinModelPortalQ4UZI9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314565.XC_0452.

Proteomic databases

PRIDEQ4UZI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY47534; AAY47534; XC_0452.
GeneID3382101.
KEGGxcb:XC_0452.
PATRIC24062142. VBIXanCam24967_0482.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycXCAM314565:GCQG-449-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_XANC8
AccessionPrimary (citable) accession number: Q4UZI9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 56 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