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UniProtKB/Swiss-Prot entry Q8PDA2


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

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Entry information
Entry name HGD_XANCP
Primary accession number Q8PDA2
Secondary accession numbers None
Integrated into Swiss-Prot on October 10, 2002
Sequence was last modified on October 10, 2002 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 36)
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: XCC0438
From
Xanthomonas campestris pv. campestris [TaxID: 340] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
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
AE012141; AAM39756.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_635832.1; -.
3D structure databases
ModBase Q8PDA2.
Enzyme and pathway databases
BioCyc XCAM190485:XCC0438-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 Q8PDA2.
Genome annotation databases
GeneID 1000916; -.
GenomeReviews AE008922_GR; XCC0438.
KEGG xcc:XCC0438; -.
Phylogenomic databases
HOGENOM Q8PDA2; -.
Genome annotation databases
CMR Q8PDA2; XCC0438.
Other
ProtoNet Q8PDA2.
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   455  455     Homogentisate 1,2-dioxygenase. PRO_0000220258
METAL   351   351        Iron (By similarity). 
METAL   357   357        Iron (By similarity). 
METAL   387   387        Iron (By similarity). 
Sequence information
Length: 455 AA [This is the length of the unprocessed precursor] Molecular weight: 50406 Da [This is the MW of the unprocessed precursor] CRC64: 2225A12DAD492A23 [This is a checksum on the sequence]
        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 

Q8PDA2 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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