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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

BNA1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Fe2+UniRule annotation

Pathway: NAD(+) biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (BNA4), Kynurenine 3-monooxygenase (BNA4)
  2. Kynureninase (BNA5), Kynureninase (BNA5)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (BNA1), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451DioxygenUniRule annotation
Metal bindingi49 – 491Iron; catalyticUniRule annotation
Metal bindingi55 – 551Iron; catalyticUniRule annotation
Binding sitei55 – 551SubstrateUniRule annotation
Metal bindingi93 – 931Iron; catalyticUniRule annotation
Binding sitei97 – 971SubstrateUniRule annotation
Binding sitei107 – 1071SubstrateUniRule annotation
Metal bindingi122 – 1221Divalent metal cationUniRule annotation
Metal bindingi125 – 1251Divalent metal cationUniRule annotation
Metal bindingi159 – 1591Divalent metal cationUniRule annotation
Metal bindingi162 – 1621Divalent metal cationUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

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
ORF Names:CaO19.3515
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0005808. orf19.3515.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1711713-hydroxyanthranilate 3,4-dioxygenasePRO_0000361984Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ59K86.
SMRiQ59K86. Positions 6-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
InParanoidiQ59K86.
KOiK00452.
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.

Q59K86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLGQPINII KWIEENGDLL KPPVNNFCLH RGGFTIMIVG GPNERSDYHI
60 70 80 90 100
NQTPEYFYQF KGTMCLKVVD DGEFKDIFIN EGDSFLLPPN VPHNPCRYEN
110 120 130 140 150
TIGIVVEQDR PAGVNDKVRW YCQKCQTVIH EVEFYLTDLG TQIKEAIVKF
160 170
DADLDARTCK NCGTVNSSRR D
Length:171
Mass (Da):19,545
Last modified:April 26, 2005 - v1
Checksum:iEAADB3DA38113136
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000315 Genomic DNA. Translation: EAK90890.1.
RefSeqiXP_710160.1. XM_705068.1.

Genome annotation databases

GeneIDi3648245.
KEGGical:CaO19.3515.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000315 Genomic DNA. Translation: EAK90890.1.
RefSeqiXP_710160.1. XM_705068.1.

3D structure databases

ProteinModelPortaliQ59K86.
SMRiQ59K86. Positions 6-169.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3648245.
KEGGical:CaO19.3515.

Organism-specific databases

CGDiCAL0005808. orf19.3515.

Phylogenomic databases

eggNOGiNOG77058.
InParanoidiQ59K86.
KOiK00452.
OrthoDBiEOG7QK0Q0.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.

Entry informationi

Entry namei3HAO_CANAL
AccessioniPrimary (citable) accession number: Q59K86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: April 26, 2005
Last modified: June 24, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.