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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

BNA1

Organism
Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
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

Pathwayi: 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)
  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; catalyticUniRule annotation1
Metal bindingi55Iron; catalyticUniRule annotation1
Binding sitei55SubstrateUniRule annotation1
Metal bindingi93Iron; catalyticUniRule annotation1
Binding sitei97SubstrateUniRule annotation1
Binding sitei107SubstrateUniRule annotation1
Metal bindingi122Divalent metal cationUniRule annotation1
Metal bindingi125Divalent metal cationUniRule annotation1
Metal bindingi159Divalent metal cationUniRule annotation1
Metal bindingi162Divalent metal cationUniRule annotation1

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:LELG_03286
OrganismiLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus)
Taxonomic identifieri379508 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeLodderomyces
Proteomesi
  • UP000001996 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003619881 – 1753-hydroxyanthranilate 3,4-dioxygenaseAdd BLAST175

Interactioni

Protein-protein interaction databases

STRINGi379508.XP_001525358.1.

Structurei

3D structure databases

ProteinModelPortaliA5E0Z9.
SMRiA5E0Z9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3995. Eukaryota.
ENOG4111GH8. LUCA.
InParanoidiA5E0Z9.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG092C5CUF.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_00825. 3_HAO. 1 hit.
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.

A5E0Z9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLPEPLNIK AWVEENEHLL KPPVNNFCLH RGGFTVMIVG GPNERSDYHI
60 70 80 90 100
NQTPEYFYQY KGTMCLKVVD EGKFRDIYIR EGDTFLLPPN VPHNPCRFEN
110 120 130 140 150
TVGIVVEQDR PKGVNDRIRW YCARCESIVC EEEFYLTDLG TQIKDAIVAF
160 170
DSNIEAKTCK NCGHVNSSKR EPAEF
Length:175
Mass (Da):20,157
Last modified:June 12, 2007 - v1
Checksum:i6ABC58FEBA0680A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981527 Genomic DNA. Translation: EDK45107.1.
RefSeqiXP_001525358.1. XM_001525308.1.

Genome annotation databases

EnsemblFungiiEDK45107; EDK45107; LELG_03286.
GeneIDi5232567.
KEGGilel:LELG_03286.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH981527 Genomic DNA. Translation: EDK45107.1.
RefSeqiXP_001525358.1. XM_001525308.1.

3D structure databases

ProteinModelPortaliA5E0Z9.
SMRiA5E0Z9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi379508.XP_001525358.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDK45107; EDK45107; LELG_03286.
GeneIDi5232567.
KEGGilel:LELG_03286.

Phylogenomic databases

eggNOGiKOG3995. Eukaryota.
ENOG4111GH8. LUCA.
InParanoidiA5E0Z9.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG092C5CUF.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_00825. 3_HAO. 1 hit.
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...

Entry informationi

Entry namei3HAO_LODEL
AccessioniPrimary (citable) accession number: A5E0Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 12, 2007
Last modified: November 2, 2016
This is version 59 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.