3-hydroxyanthranilate 3,4-dioxygenase - Saccharomyces cerevisiae (Baker's yeast)

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

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

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

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Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	de novo NAD biosynthetic process from tryptophan Inferred from genetic interaction. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxyanthranilate 3,4-dioxygenase activity Ref.4 Inferred from mutant phenotype. Source: SGD iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 177

177

3-hydroxyanthranilate 3,4-dioxygenase

PRO_0000064375

Sites

Metal binding

Iron; catalytic

Metal binding

Iron; catalytic

Metal binding

Iron; catalytic

Metal binding

126

Divalent metal cation

Metal binding

129

Divalent metal cation

Metal binding

163

Divalent metal cation

Metal binding

166

Divalent metal cation

Binding site

Dioxygen By similarity

Binding site

Substrate By similarity

Binding site

101

Substrate By similarity

Binding site

111

Substrate By similarity

Amino acid modifications

Modified residue

176

Phosphoserine Ref.7 Ref.8 Ref.9

Secondary structure

177

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P47096-1 [UniParc].

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

177

20,235

        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

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References

	« Hide 'large scale' referencesShow '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. 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. 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.

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Cross-references

Sequence databases

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

PIR

S57043.

RefSeq

NP_012559.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZVF	X-ray	2.41	A/B	1-175	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4759N.

IntAct

P47096. 4 interactions.

Proteomic databases

PeptideAtlas

P47096.

PRIDE

P47096.

Genome annotation databases

Ensembl

YJR025C. Saccharomyces cerevisiae. [Contig view]

GeneID

853482.

GenomeReviews

Gene locus YJR025C in contig Y13136_GR.

KEGG

sce:YJR025C.

NMPDR

fig|4932.3.peg.3533.

Organism-specific databases

CYGD

YJR025c.

SGD

S000003786. BNA1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P47096.

OMA

P47096. RHSPQRP.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-8161.

BRENDA

1.13.11.6. 250.

Gene expression databases

ArrayExpress

P47096.

GermOnline

YJR025C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR010329. 3hydroanth_dOase.
[Graphical view]

Pfam

PF06052. 3-HAO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03037. anthran_nbaC. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

974095.

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Entry information

Entry name

3HAO_YEAST

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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