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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

BNA1

Organism
Coccidioides immitis (strain RS) (Valley fever fungus)
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)
  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 sitei50 – 501DioxygenUniRule annotation
Metal bindingi54 – 541Iron; catalyticUniRule annotation
Metal bindingi60 – 601Iron; catalyticUniRule annotation
Binding sitei60 – 601SubstrateUniRule annotation
Metal bindingi102 – 1021Iron; catalyticUniRule annotation
Binding sitei106 – 1061SubstrateUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation
Metal bindingi131 – 1311Divalent metal cationUniRule annotation
Metal bindingi134 – 1341Divalent metal cationUniRule annotation
Metal bindingi168 – 1681Divalent metal cationUniRule annotation
Metal bindingi171 – 1711Divalent 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:CIMG_02183
OrganismiCoccidioides immitis (strain RS) (Valley fever fungus)
Taxonomic identifieri246410 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides
ProteomesiUP000001261 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:CIMG_02183.

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 – 1921923-hydroxyanthranilate 3,4-dioxygenasePRO_0000361986Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi246410.XP_001248412.1.

Structurei

3D structure databases

ProteinModelPortaliQ1E5I0.
SMRiQ1E5I0. Positions 5-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

InParanoidiQ1E5I0.
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.

Q1E5I0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAPALNLPK WLEENSHLLQ PPINNYCVYH PSAPATQGYT VMVVGGPNVR
60 70 80 90 100
TDYHINPTPE FFYQHRGSML LRTVDQSTSP PTFQDIPIHE GSLFLLPANT
110 120 130 140 150
PHCPVRFADT VGVVLEVPRP ENATDCMRWY CKGCGEIVWE KKFHCTDLGT
160 170 180 190
QVKEVVEEFA ADDEKRKCKA CGSVRSVRYE DGEVVQPPRA PE
Length:192
Mass (Da):21,611
Last modified:July 11, 2006 - v1
Checksum:i00503228EB6FC03A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG704911 Genomic DNA. Translation: EAS36973.2.
RefSeqiXP_001248412.1. XM_001248411.2.
XP_001248556.1. XM_001248555.2.

Genome annotation databases

GeneIDi4566696.
4567554.
KEGGicim:CIMG_02183.
cim:CIMG_02327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG704911 Genomic DNA. Translation: EAS36973.2.
RefSeqiXP_001248412.1. XM_001248411.2.
XP_001248556.1. XM_001248555.2.

3D structure databases

ProteinModelPortaliQ1E5I0.
SMRiQ1E5I0. Positions 5-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246410.XP_001248412.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4566696.
4567554.
KEGGicim:CIMG_02183.
cim:CIMG_02327.

Organism-specific databases

EuPathDBiFungiDB:CIMG_02183.

Phylogenomic databases

InParanoidiQ1E5I0.
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RS.
  2. Cited for: GENOME REANNOTATION.
    Strain: RS.

Entry informationi

Entry namei3HAO_COCIM
AccessioniPrimary (citable) accession number: Q1E5I0
Secondary accession number(s): J3KL46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 11, 2006
Last modified: June 24, 2015
This is version 61 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

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.