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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: -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.

Miscellaneous

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

Catalytic activityi

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.UniRule annotation1 Publication

Cofactori

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (BNA4)
  2. Kynureninase (BNA5)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (BNA1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45DioxygenUniRule annotation1
Metal bindingi49Iron; catalytic1
Metal bindingi55Iron; catalytic1
Binding sitei55SubstrateUniRule annotation1
Metal bindingi97Iron; catalytic1
Binding sitei101SubstrateUniRule annotation1
Binding sitei111SubstrateUniRule annotation1
Metal bindingi126Divalent metal cation1
Metal bindingi129Divalent metal cation1
Metal bindingi163Divalent metal cation1
Metal bindingi166Divalent metal cation1

GO - Molecular functioni

  • 3-hydroxyanthranilate 3,4-dioxygenase activity Source: SGD
  • iron ion binding Source: InterPro

GO - Biological processi

  • 'de novo' NAD biosynthetic process from tryptophan Source: SGD

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processPyridine nucleotide biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YJR025C-MONOMER
YEAST:YJR025C-MONOMER
BRENDAi1.13.11.6 984
ReactomeiR-SCE-71240 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
Proteomesi

Organism-specific databases

EuPathDBiFungiDB:YJR025C
SGDiS000003786 BNA1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000643751 – 1773-hydroxyanthranilate 3,4-dioxygenaseAdd BLAST177

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei176PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP47096
PaxDbiP47096
PRIDEiP47096

PTM databases

iPTMnetiP47096

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi33778, 108 interactors
DIPiDIP-4759N
IntActiP47096, 1 interactor
MINTiP47096
STRINGi4932.YJR025C

Structurei

Secondary structure

1177
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 16Combined sources8
Helixi17 – 20Combined sources4
Beta strandi21 – 24Combined sources4
Beta strandi26 – 30Combined sources5
Beta strandi32 – 39Combined sources8
Beta strandi41 – 43Combined sources3
Beta strandi48 – 50Combined sources3
Beta strandi55 – 62Combined sources8
Beta strandi64 – 70Combined sources7
Beta strandi72 – 75Combined sources4
Beta strandi77 – 83Combined sources7
Beta strandi87 – 91Combined sources5
Beta strandi97 – 101Combined sources5
Beta strandi106 – 112Combined sources7
Beta strandi116 – 118Combined sources3
Beta strandi121 – 125Combined sources5
Turni127 – 129Combined sources3
Beta strandi132 – 137Combined sources6
Beta strandi140 – 142Combined sources3
Helixi145 – 155Combined sources11
Helixi158 – 161Combined sources4
Turni164 – 166Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP47096

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000013008
HOGENOMiHOG000218448
InParanoidiP47096
KOiK00452
OMAiNARKDYH
OrthoDBiEOG092C5CUF

Family and domain databases

Gene3Di2.60.120.10, 1 hit
HAMAPiMF_00825 3_HAO, 1 hit
InterProiView protein in InterPro
IPR010329 3hydroanth_dOase
IPR014710 RmlC-like_jellyroll
IPR011051 RmlC_Cupin_sf
PANTHERiPTHR15497 PTHR15497, 1 hit
PfamiView protein in Pfam
PF06052 3-HAO, 1 hit
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

Entry informationi

Entry namei3HAO_YEAST
AccessioniPrimary (citable) accession number: P47096
Secondary accession number(s): D6VWJ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 23, 2018
This is version 156 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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