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Reviewed, UniProtKB/Swiss-Prot P47096 (3HAO_YEAST)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-hydroxyanthranilate 3,4-dioxygenase
    EC=1.13.11.6
Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
      Short name=HAD
    3-hydroxyanthranilate oxygenase
      Short name=3-HAO
    Biosynthesis of nicotinic acid protein 1
Gene names
Name: BNA1
Synonyms: HAD1
Ordered Locus Names: YJR025C
ORF Names: J1550
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.

Catalytic activity

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. Ref.4

Cofactor

Fe2+ ion.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; pyridine-2,3-dicarboxylate from L-kynurenine: step 3/3. Ref.4

Subunit structure

Homodimer. Ref.10

Subcellular location

Cytoplasm. Nucleus. Ref.5

Miscellaneous

Present with 2330 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the 3-HAO family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1771773-hydroxyanthranilate 3,4-dioxygenase
PRO_0000064375

Sites

Metal binding491Iron; catalytic
Metal binding551Iron; catalytic
Metal binding971Iron; catalytic
Metal binding1261Divalent metal cation
Metal binding1291Divalent metal cation
Metal binding1631Divalent metal cation
Metal binding1661Divalent metal cation
Binding site451Dioxygen By similarity
Binding site551Substrate By similarity
Binding site1011Substrate By similarity
Binding site1111Substrate By similarity

Amino acid modifications

Modified residue1761Phosphoserine Ref.7 Ref.8 Ref.9

Secondary structure

........................................... 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47096-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 930D69F486632417

FASTA17720,235
        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 

« Hide

References

« Hide 'large scale' references
[1]"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."
Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J., Herbert C.J.
Yeast 11:1179-1186(1995) [PubMed: 8619316] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
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. expand/collapse author list , 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.
EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis."
Kucharczyk R., Zagulski M., Rytka J., Herbert C.J.
FEBS Lett. 424:127-130(1998) [PubMed: 9539135] [Abstract]
Cited for: CATALYTIC ACTIVITY, PATHWAY.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY.
[10]"Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases."
Li X., Guo M., Fan J., Tang W., Wang D., Ge H., Rong H., Teng M., Niu L., Liu Q., Hao Q.
Protein Sci. 15:761-773(2006) [PubMed: 16522801] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-175 IN COMPLEX WITH DIVALENT METAL IONS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z49525 Genomic DNA. Translation: CAA89550.1.
X87297 Genomic DNA. Translation: CAA60720.1.
AY558309 Genomic DNA. Translation: AAS56635.1.
PIRS57043.
RefSeqNP_012559.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ZVFX-ray2.41A/B1-175[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4759N.
IntActP47096. 4 interactions.

Proteomic databases

PeptideAtlasP47096.
PRIDEP47096.

Genome annotation databases

EnsemblYJR025C. Saccharomyces cerevisiae. [Contig view]
GeneID853482.
GenomeReviewsGene locus YJR025C in contig Y13136_GR.
KEGGsce:YJR025C.
NMPDRfig|4932.3.peg.3533.

Organism-specific databases

CYGDYJR025c.
SGDS000003786. BNA1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP47096.
OMAP47096. RHSPQRP.

Enzyme and pathway databases

BioCycMetaCyc:MON-8161.
BRENDA1.13.11.6. 250.

Gene expression databases

ArrayExpressP47096.
GermOnlineYJR025C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR010329. 3hydroanth_dOase.
[Graphical view]
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

Other Resources

NextBio974095.

Entry information

Entry name3HAO_YEAST
AccessionPrimary (citable) accession number: P47096
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents