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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Pseudomonas fluorescens
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

Fe2+1 PublicationNote: Binds 2 Fe2+ ions per subunit.1 Publication

Enzyme regulationi

Inhibited by Zn2+, Cu2+ and Cd2+.1 Publication

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 (kmo)
  2. Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (kynU), Kynureninase (HZ99_03140)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (nbaC)
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 sitei48DioxygenUniRule annotation1
Metal bindingi52Iron 1; catalyticCurated1
Metal bindingi58Iron 1; catalyticUniRule annotation1
Binding sitei58SubstrateUniRule annotation1
Metal bindingi96Iron 1; catalyticCurated1
Binding sitei100SubstrateUniRule annotation1
Binding sitei111SubstrateUniRule annotation1
Metal bindingi126Iron 2UniRule annotation1
Metal bindingi129Iron 2UniRule annotation1
Metal bindingi163Iron 2UniRule annotation1
Metal bindingi166Iron 2UniRule 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

BioCyciMetaCyc:MONOMER-13359.
BRENDAi1.13.11.6. 5121.
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
Gene namesi
Name:nbaCUniRule annotation
OrganismiPseudomonas fluorescens
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52H → A: Loss of activity. 1 Publication1
Mutagenesisi96H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002454721 – 1853-hydroxyanthranilate 3,4-dioxygenaseAdd BLAST185

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ83V26.
SMRiQ83V26.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

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.

Q83V26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFTFGKPLN FQRWLDDHSD LLRPPVGNQQ VWQDSDFIVT VVGGPNFRTD
60 70 80 90 100
FHDDPMEEFF YQFKGNAYLN IMDRGQMDRV ELKEGDIFLL PPHLRHSPQR
110 120 130 140 150
PEAGSRCLVI ERQRPKGMLD GFEWYCLSCN GLVYRVDVQL NSIVTDLPPL
160 170 180
FDIFYGNVGL RKCPQCGQVH PGKAAIEAVA RGDQP
Length:185
Mass (Da):21,245
Last modified:June 1, 2003 - v1
Checksum:iAC932875CC9D3D7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088043 Genomic DNA. Translation: BAC65311.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088043 Genomic DNA. Translation: BAC65311.1.

3D structure databases

ProteinModelPortaliQ83V26.
SMRiQ83V26.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.
BioCyciMetaCyc:MONOMER-13359.
BRENDAi1.13.11.6. 5121.

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_PSEFL
AccessioniPrimary (citable) accession number: Q83V26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.