3-hydroxyanthranilate 3,4-dioxygenase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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

Last modified April 3, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
3-hydroxyanthranilate 3,4-dioxygenase
EC=1.13.11.6

Alternative name(s):
3-hydroxyanthranilate oxygenase
Short name=3-HAO
3-hydroxyanthranilic acid dioxygenase
Short name=HAD
Biosynthesis of nicotinic acid protein 1

Gene names

Name:	BNA1
Synonyms:	HAD1
Ordered Locus Names:	YJR025C
ORF Names:	J1550

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP-Rule MF_03019
Catalytic activity	3-hydroxyanthranilate + O₂ = 2-amino-3-carboxymuconate semialdehyde. Ref.5
Cofactor	Fe²⁺ ion.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. Ref.5
Subunit structure	Homodimer. Ref.11
Subcellular location	Cytoplasm. Nucleus Ref.6.
Miscellaneous	Present with 2330 molecules/cell in log phase SD medium. HAMAP-Rule MF_03019
Sequence similarities	Belongs to the 3-HAO family.

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 Reference proteome
Gene Ontology (GO)
Biological_process	de novo NAD biosynthetic process from tryptophan Inferred from genetic interaction PubMed 12062417. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 11901108. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from mutant phenotype Ref.5. Source: SGD iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 177

177

3-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019

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.8 Ref.9 Ref.10

Secondary structure

177

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P47096 [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

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, PATHWAY.
[6]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY. Strain: YAL6B.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY. Strain: ADR376.
[10]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY.
[11]	"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] [Europe PMC] [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

EMBL
GenBank
DDBJ

Z49525 Genomic DNA. Translation: CAA89550.1.
X87297 Genomic DNA. Translation: CAA60720.1.
AY558309 Genomic DNA. Translation: AAS56635.1.
BK006943 Genomic DNA. Translation: DAA08814.1.

PIR

S57043.

RefSeq

NP_012559.1. NM_001181683.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P47096.

SMR

P47096. Positions 1-175.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4759N.

IntAct

P47096. 1 interaction.

MINT

MINT-529506.

STRING

4932.YJR025C.

Proteomic databases

PaxDb

P47096.

PeptideAtlas

P47096.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJR025C; YJR025C; YJR025C.

GeneID

853482.

KEGG

sce:YJR025C.

Organism-specific databases

CYGD

YJR025c.

SGD

S000003786. BNA1.

Phylogenomic databases

eggNOG

NOG77058.

GeneTree

ENSGT00390000013008.

HOGENOM

HOG000218448.

K00452.

OMA

HSPQRPE.

OrthoDB

EOG476P8N.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-8161.

BRENDA

1.13.11.6. 984.

UniPathway

UPA00253; UER00330.

Gene expression databases

Genevestigator

P47096.

GermOnline

YJR025C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.60.120.10. 1 hit.

HAMAP

MF_00825. 3_HAO.

InterPro

IPR010329. 3hydroanth_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]

PANTHER

PTHR15497. PTHR15497. 1 hit.

Pfam

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

SUPFAM

SSF51182. RmlC_like_cupin. 1 hit.

TIGRFAMs

TIGR03037. anthran_nbaC. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P47096.

NextBio

974095.

Entry information

Entry name

3HAO_YEAST

Accession

Primary (citable) accession number: P47096
Secondary accession number(s): D6VWJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome X

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

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents