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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

BNA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.1 PublicationUniRule annotation

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451DioxygenUniRule annotation
Metal bindingi49 – 491Iron; catalytic
Metal bindingi55 – 551Iron; catalytic
Binding sitei55 – 551SubstrateUniRule annotation
Metal bindingi97 – 971Iron; catalytic
Binding sitei101 – 1011SubstrateUniRule annotation
Binding sitei111 – 1111SubstrateUniRule annotation
Metal bindingi126 – 1261Divalent metal cation
Metal bindingi129 – 1291Divalent metal cation
Metal bindingi163 – 1631Divalent metal cation
Metal bindingi166 – 1661Divalent metal cation

GO - Molecular functioni

  1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: SGD
  2. ferrous iron binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: SGD
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  4. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8161.
YEAST:YJR025C-MONOMER.
BRENDAi1.13.11.6. 984.
ReactomeiREACT_230831. Tryptophan catabolism.
UniPathwayiUPA00253; UER00330.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyanthranilate 3,4-dioxygenaseUniRule annotation (EC:1.13.11.6UniRule annotation)
Alternative name(s):
3-hydroxyanthranilate oxygenaseUniRule annotation
Short name:
3-HAOUniRule annotation
3-hydroxyanthranilic acid dioxygenaseUniRule annotation
Short name:
HADUniRule annotation
Biosynthesis of nicotinic acid protein 1UniRule annotation
Gene namesi
Name:BNA1UniRule annotation
Synonyms:HAD1
Ordered Locus Names:YJR025C
ORF Names:J1550
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR025c.
SGDiS000003786. BNA1.

Subcellular locationi

Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1771773-hydroxyanthranilate 3,4-dioxygenasePRO_0000064375Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47096.
PaxDbiP47096.
PeptideAtlasiP47096.

Expressioni

Gene expression databases

GenevestigatoriP47096.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi33778. 48 interactions.
DIPiDIP-4759N.
IntActiP47096. 1 interaction.
MINTiMINT-529506.
STRINGi4932.YJR025C.

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 168Combined sources
Helixi17 – 204Combined sources
Beta strandi21 – 244Combined sources
Beta strandi26 – 305Combined sources
Beta strandi32 – 398Combined sources
Beta strandi41 – 433Combined sources
Beta strandi48 – 503Combined sources
Beta strandi55 – 628Combined sources
Beta strandi64 – 707Combined sources
Beta strandi72 – 754Combined sources
Beta strandi77 – 837Combined sources
Beta strandi87 – 915Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi121 – 1255Combined sources
Turni127 – 1293Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi140 – 1423Combined sources
Helixi145 – 15511Combined sources
Helixi158 – 1614Combined sources
Turni164 – 1663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZVFX-ray2.41A/B1-175[»]
ProteinModelPortaliP47096.
SMRiP47096. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47096.

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
GeneTreeiENSGT00390000013008.
HOGENOMiHOG000218448.
InParanoidiP47096.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG7QK0Q0.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_00825. 3_HAO.
InterProiIPR010329. 3hydroanth_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR15497. PTHR15497. 1 hit.
PfamiPF06052. 3-HAO. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.

Sequencei

Sequence statusi: Complete.

P47096-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFNTTPINID KWLKENEGLL KPPVNNYCLH KGGFTVMIVG GPNERTGYHI
60 70 80 90 100
NPTPEWFYQK KGSMLLKVVD ETDAEPKFID IIINEGDSYL LPGNVPHSPV
110 120 130 140 150
RFADTVGIVV EQDRPGGEND KIRWYCSHCR QVVHESELQM LDLGTQVKEA
160 170
ILDFENDVEK RTCFHCKTLN YARPQSN
Length:177
Mass (Da):20,235
Last modified:February 1, 1996 - v1
Checksum:i930D69F486632417
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49525 Genomic DNA. Translation: CAA89550.1.
X87297 Genomic DNA. Translation: CAA60720.1.
AY558309 Genomic DNA. Translation: AAS56635.1.
BK006943 Genomic DNA. Translation: DAA08814.1.
PIRiS57043.
RefSeqiNP_012559.1. NM_001181683.1.

Genome annotation databases

EnsemblFungiiYJR025C; YJR025C; YJR025C.
GeneIDi853482.
KEGGisce:YJR025C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49525 Genomic DNA. Translation: CAA89550.1.
X87297 Genomic DNA. Translation: CAA60720.1.
AY558309 Genomic DNA. Translation: AAS56635.1.
BK006943 Genomic DNA. Translation: DAA08814.1.
PIRiS57043.
RefSeqiNP_012559.1. NM_001181683.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZVFX-ray2.41A/B1-175[»]
ProteinModelPortaliP47096.
SMRiP47096. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33778. 48 interactions.
DIPiDIP-4759N.
IntActiP47096. 1 interaction.
MINTiMINT-529506.
STRINGi4932.YJR025C.

Proteomic databases

MaxQBiP47096.
PaxDbiP47096.
PeptideAtlasiP47096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR025C; YJR025C; YJR025C.
GeneIDi853482.
KEGGisce:YJR025C.

Organism-specific databases

CYGDiYJR025c.
SGDiS000003786. BNA1.

Phylogenomic databases

eggNOGiNOG77058.
GeneTreeiENSGT00390000013008.
HOGENOMiHOG000218448.
InParanoidiP47096.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG7QK0Q0.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.
BioCyciMetaCyc:MONOMER-8161.
YEAST:YJR025C-MONOMER.
BRENDAi1.13.11.6. 984.
ReactomeiREACT_230831. Tryptophan catabolism.

Miscellaneous databases

EvolutionaryTraceiP47096.
NextBioi974095.
PROiP47096.

Gene expression databases

GenevestigatoriP47096.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_00825. 3_HAO.
InterProiIPR010329. 3hydroanth_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR15497. PTHR15497. 1 hit.
PfamiPF06052. 3-HAO. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.

Entry informationi

Entry namei3HAO_YEAST
AccessioniPrimary (citable) accession number: P47096
Secondary accession number(s): D6VWJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2330 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.