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UniProtKB/Swiss-Prot entry P47096


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

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Entry information
Entry name 3HAO_YEAST
Primary accession number P47096
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 71)
Name and origin of the protein
Protein name 3-hydroxyanthranilate 3,4-dioxygenase
Synonyms EC 1.13.11.6
3-hydroxyanthranilic acid dioxygenase
3-hydroxyanthranilate oxygenase
3-HAO
Biosynthesis of nicotinic acid protein 1
Gene name
Name: BNA1
Synonyms: HAD1
OrderedLocusNames: YJR025C
ORFNames: J1550
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/yea.320111208; PubMed=8619316 [NCBI, ExPASy, EBI, Israel, Japan]
Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J., Herbert C.J.;
"The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon.";
Yeast 11:1179-1186(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
CATALYTIC ACTIVITY, AND PATHWAY.
DOI=10.1016/S0014-5793(98)00153-7; PubMed=9539135 [NCBI, ExPASy, EBI, Israel, Japan]
Kucharczyk R., Zagulski M., Rytka J., Herbert C.J.;
"The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis.";
FEBS Lett. 424:127-130(1998).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-175 IN COMPLEX WITH DIVALENT METAL IONS, AND SUBUNIT.
DOI=10.1110/ps.051967906; PubMed=16522801 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Guo M., Fan J., Tang W., Wang D., Ge H., Rong H., Teng M., Niu L., Liu Q., Hao Q.;
"Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases.";
Protein Sci. 15:761-773(2006).
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
Z49525; CAA89550.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X87297; CAA60720.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558309; AAS56635.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S57043; S57043.
RefSeq NP_012559.1; -.
3D structure databases
PDB
1ZVF; X-ray; 2.41 A; A/B=1-175.[ExPASy / RCSB / EBI]
PDBsum 1ZVF; -.
ModBase P47096.
Protein-protein interaction databases
DIP DIP:4759N; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-8161; -.
Organism-specific databases
CYGD YJR025c; -.
SGD S000003786; BNA1.
Yeast-GFP YJR025C.
Gene expression databases
ArrayExpress P47096; -.
GermOnline YJR025C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0000334; Molecular function: 3-hydroxyanthranilate 3,4-dioxygenase activity (inferred from mutant phenotype from SGD).
GO:0034354; Biological process: de novo NAD biosynthetic process from tryptophan (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR010329; 3hydroanth_dOase.
Graphical view of domain structure.
Pfam PF06052; 3-HAO; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR03037; anthran_nbaC; 1.
BLOCKS P47096.
Proteomic databases
PeptideAtlas P47096; -.
Genome annotation databases
Ensembl YJR025C; Saccharomyces cerevisiae. [Contig view]
GeneID 853482; -.
GenomeReviews Y13136_GR; YJR025C.
KEGG sce:YJR025C; -.
NMPDR fig|4932.3.peg.3533; -.
Phylogenomic databases
HOGENOM P47096; -.
Other
LinkHub P47096; -.
ProtoNet P47096.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   177  177     3-hydroxyanthranilate 3,4-dioxygenase. PRO_0000064375
METAL   49    49        Iron; catalytic. 
METAL   55    55        Iron; catalytic. 
METAL   97    97        Iron; catalytic. 
METAL   126   126        Divalent metal cation. 
METAL   129   129        Divalent metal cation. 
METAL   163   163        Divalent metal cation. 
METAL   166   166        Divalent metal cation. 
BINDING   45    45        Dioxygen (By similarity). 
BINDING   55    55        Substrate (By similarity). 
BINDING   101   101        Substrate (By similarity). 
BINDING   111   111        Substrate (By similarity). 
MOD_RES   176   176        Phosphoserine. 
HELIX   9    16  8      
HELIX   17    20  4      
STRAND   21    24  4      
STRAND   26    30  5      
STRAND   32    39  8      
STRAND   41    43  3      
STRAND   48    50  3      
STRAND   55    62  8      
STRAND   64    70  7      
STRAND   72    75  4      
STRAND   77    83  7      
STRAND   87    91  5      
STRAND   97   101  5      
STRAND   106   112  7      
STRAND   116   118  3      
STRAND   121   125  5      
TURN   127   129  3      
STRAND   132   137  6      
STRAND   140   142  3      
HELIX   145   155  11      
HELIX   158   161  4      
TURN   164   166  3      
Sequence information
Length: 177 AA [This is the length of the unprocessed precursor] Molecular weight: 20235 Da [This is the MW of the unprocessed precursor] CRC64: 930D69F486632417 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFNTTPINID KWLKENEGLL KPPVNNYCLH KGGFTVMIVG GPNERTGYHI NPTPEWFYQK 

        70         80         90        100        110        120 
KGSMLLKVVD ETDAEPKFID IIINEGDSYL LPGNVPHSPV RFADTVGIVV EQDRPGGEND 

       130        140        150        160        170 
KIRWYCSHCR QVVHESELQM LDLGTQVKEA ILDFENDVEK RTCFHCKTLN YARPQSN 

P47096 in FASTA format

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