ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q2NYM7

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HGD_XANOM
Primary accession number Q2NYM7
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on February 7, 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: XOO3845
From
Xanthomonas oryzae pv. oryzae (strain MAFF 311018) [TaxID: 342109] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
"Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity.";
Jpn. Agric. Res. Q. 39:275-287(2005).
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
AP008229; BAE70600.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_452874.1; -.
3D structure databases
ModBase Q2NYM7.
Enzyme and pathway databases
BioCyc XORY342109:XOO3845-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 Q2NYM7.
Genome annotation databases
GeneID 3858339; -.
GenomeReviews AP008229_GR; XOO3845.
KEGG xom:XOO_3845; -.
Phylogenomic databases
HOGENOM Q2NYM7; -.
Genome annotation databases
CMR Q2NYM7; XOO3845.
Other
ProtoNet Q2NYM7.
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   441  441     Homogentisate 1,2-dioxygenase. PRO_1000019545
METAL   330   330        Iron (By similarity). 
METAL   336   336        Iron (By similarity). 
METAL   366   366        Iron (By similarity). 
Sequence information
Length: 441 AA [This is the length of the unprocessed precursor] Molecular weight: 48542 Da [This is the MW of the unprocessed precursor] CRC64: 05CF74A5847A7698 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MHNPQHYMTG FGNEFATEAV AGSLPVGQNS PQRVAHGLYA EQLSGTAFTA PRGENRRSWL 

        70         80         90        100        110        120 
YRIRPAAVHG RFSLIEQSRL HNDFGGGPVP PDQMRWSPLP LPATPTDFVD GLYTMAGNGS 

       130        140        150        160        170        180 
PEAMTGVAVH LYAANASMHG RFFYNADGEL LLVPQLGRLR VCTELGVLEL EPQQIGVIPR 

       190        200        210        220        230        240 
GVRFRVELLD SAARGYVCEN FGGLLRLPDL GPIGANGLAN PRDFETPRAA FEQRDGAFEL 

       250        260        270        280        290        300 
VAKFQGHLWR ADIDHSPLDV VAWHGNYAPY RYDLRRFNTI GSISFDHPDP SIFTVLTSPS 

       310        320        330        340        350        360 
DTHGTANMDF AIFPPRWLVA QHTFRPPWFH RNVASEFMGL VHGVYDAKAE GFAPGGASLH 

       370        380        390        400        410        420 
NCMSGHGPDA ATFDKASQAD LTRPDVIAET MAFMFETRAV LRPTQQALSA AHRQADYQQC 

       430        440 
WSGLRAAFQH PPAKNTTSVL R
Q2NYM7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!