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UniProtKB/Swiss-Prot entry Q2SYQ6

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HGD_BURTA
Primary accession number Q2SYQ6
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on January 24, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 20)
Name and origin of the protein
Protein name Homogentisate 1,2-dioxygenase
Synonyms EC 1.13.11.5
Homogentisicase
Homogentisate oxygenase
Homogentisic acid oxidase
Gene name
Name: hmgA
OrderedLocusNames: BTH_I1397
From
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [TaxID: 271848] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000086; ABC36904.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_441943.1; -.
3D structure databases
ModBase Q2SYQ6.
Enzyme and pathway databases
BioCyc BTHA271848:BTH_I1397-MON; -.
Ontologies
GO
GO:0004411; Molecular function: homogentisate 1,2-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from HAMAP).
GO:0006559; Biological process: L-phenylalanine catabolic process (inferred from electronic annotation from HAMAP).
GO:0006572; Biological process: tyrosine catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00334; -; 1.
PBIL [Tree]
InterPro IPR005708; Homogentis_dOase.
Graphical view of domain structure.
PANTHER PTHR11056; Homogentis_dOase; 1.
Pfam PF04209; HgmA; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01015; hmgA; 1.
BLOCKS Q2SYQ6.
Genome annotation databases
GeneID 3846832; -.
GenomeReviews CP000086_GR; BTH_I1397.
KEGG bte:BTH_I1397; -.
TIGR BTH_I1397; -.
Phylogenomic databases
HOGENOM Q2SYQ6; -.
Other
ProtoNet Q2SYQ6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism; Tyrosine catabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   450  450     Homogentisate 1,2-dioxygenase. PRO_1000019528
METAL   347   347        Iron (By similarity). 
METAL   353   353        Iron (By similarity). 
METAL   383   383        Iron (By similarity). 
Sequence information
Length: 450 AA [This is the length of the unprocessed precursor] Molecular weight: 50013 Da [This is the MW of the unprocessed precursor] CRC64: 32406319EE771859 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MERTTIMTLD FSKPGEAGYQ SGFANEFATE ALPGALPHAR NSPQRAPYGL YAEQLSGTAF 

        70         80         90        100        110        120 
TAPRGHNRRS WLYRIRPAAV HRPFELVSGE RRIVADFGDS GDVPPTPPNQ LRWDPLPMPA 

       130        140        150        160        170        180 
QPTDFVDGWV TMAGNGSAAA MSGCAIHLYA ANRSMRERFF YSADGELLIV PQEGRLFIMT 

       190        200        210        220        230        240 
ELGRLDVEPF EIAVIPRGVR FAVALPDGRA RGYVCENFGA LLRLPDLGPI GSNGLANPRD 

       250        260        270        280        290        300 
FLTPNASYED REGAFELVAK LNGRLWRADI DHSPFDVVAW HGNYAPYKYD LRHFNTIGSI 

       310        320        330        340        350        360 
SYDHPDPSIF LVLQSQSDTP GVDAIDFVIF PPRWLAAEDT FRPPWFHRNV ASEFMGLVHG 

       370        380        390        400        410        420 
VYDAKAEGFV PGGASLHNCM SGHGPDADTF EKASAIDTSR PNKVGDTMAF MFETRTLIRP 

       430        440        450 
TRFALDTAQL QANYFECWQG LKKHFNPEQR
Q2SYQ6 in FASTA format

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