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Protein

3-hydroxyanthranilate 3,4-dioxygenase 1

Gene

bna1-1

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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 2 (bna5-2), Kynureninase 1 (bna5-1)
  3. 3-hydroxyanthranilate 3,4-dioxygenase 1 (bna1-1), 3-hydroxyanthranilate 3,4-dioxygenase 2 (bna1-2)
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 sitei50DioxygenUniRule annotation1
Metal bindingi54Iron; catalyticUniRule annotation1
Metal bindingi60Iron; catalyticUniRule annotation1
Binding sitei60SubstrateUniRule annotation1
Metal bindingi102Iron; catalyticUniRule annotation1
Binding sitei106SubstrateUniRule annotation1
Binding sitei116SubstrateUniRule annotation1
Metal bindingi131Divalent metal cationUniRule annotation1
Metal bindingi134Divalent metal cationUniRule annotation1
Metal bindingi168Divalent metal cationUniRule annotation1
Metal bindingi171Divalent 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-dioxygenase 1UniRule annotation (EC:1.13.11.6UniRule annotation)
Alternative name(s):
3-hydroxyanthranilate oxygenase 1UniRule annotation
Short name:
3-HAO-1UniRule annotation
3-hydroxyanthranilic acid dioxygenase 1UniRule annotation
Short name:
HAD-1UniRule annotation
Biosynthesis of nicotinic acid protein 1-1UniRule annotation
Gene namesi
Name:bna1-1
ORF Names:AFUA_8G04650
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiFungiDB:Afu8g04650.

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_00003619781 – 1923-hydroxyanthranilate 3,4-dioxygenase 1Add BLAST192

Structurei

3D structure databases

ProteinModelPortaliQ4WCF1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000218448.
InParanoidiQ4WCF1.
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.

Q4WCF1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPPALNIPK WLEENSHLLQ PPVNNYCVYH PSSPATAGYT VMIVGGPNAR
60 70 80 90 100
TDYHINTTPE FFYQYRGSML LKTVDTSVSP PVFQDIPIHE GSIFLLPANT
110 120 130 140 150
PHCPVRFKDT VGVVMEQPRP KDAVDTMLWF CKKCGEVVWE KRFVCTDLGT
160 170 180 190
QVKEVVEEFA ADQEKRTCKA CGTIAETRYQ EGEVVQPPRF LE
Length:192
Mass (Da):21,705
Last modified:July 5, 2005 - v1
Checksum:i148D406C365727F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000013 Genomic DNA. Translation: EAL85233.1.
RefSeqiXP_747271.1. XM_742178.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003260; CADAFUAP00003260; CADAFUAG00003260.
GeneIDi3504643.
KEGGiafm:AFUA_8G04650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000013 Genomic DNA. Translation: EAL85233.1.
RefSeqiXP_747271.1. XM_742178.1.

3D structure databases

ProteinModelPortaliQ4WCF1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00003260; CADAFUAP00003260; CADAFUAG00003260.
GeneIDi3504643.
KEGGiafm:AFUA_8G04650.

Organism-specific databases

EuPathDBiFungiDB:Afu8g04650.

Phylogenomic databases

HOGENOMiHOG000218448.
InParanoidiQ4WCF1.
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 namei3HAO1_ASPFU
AccessioniPrimary (citable) accession number: Q4WCF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 5, 2005
Last modified: October 5, 2016
This is version 86 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.