Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
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 annotationNote: Binds 2 Fe2+ ions per subunit.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 (kmo)
  2. Kynureninase (kynU)
  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 sitei44DioxygenUniRule annotation1
Metal bindingi48Iron 1; catalyticUniRule annotation1
Metal bindingi54Iron 1; catalyticUniRule annotation1
Binding sitei54SubstrateUniRule annotation1
Metal bindingi92Iron 1; catalyticUniRule annotation1
Binding sitei96SubstrateUniRule annotation1
Binding sitei106SubstrateUniRule annotation1
Metal bindingi121Iron 2UniRule annotation1
Metal bindingi124Iron 2UniRule annotation1
Metal bindingi158Iron 2UniRule annotation1
Metal bindingi161Iron 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

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
Ordered Locus Names:XOO2302
OrganismiXanthomonas oryzae pv. oryzae (strain MAFF 311018)
Taxonomic identifieri342109 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002454831 – 1763-hydroxyanthranilate 3,4-dioxygenaseAdd BLAST176

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ2P320.
SMRiQ2P320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

KOiK00452.
OrthoDBiPOG091H0LPR.

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.

Q2P320-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD
60 70 80 90 100
EGPEWFFQLE GEMVLKVQDD GVARDIPIRA GEIFLLPPRV PHSPQRAAGS
110 120 130 140 150
IGIVIERVRL PHEQDGLQWY CPQCNHKLYE AMFPLKNIET DFPPVFDHFY
160 170
RSLALRTCSQ CGHLHPAPER YAAVED
Length:176
Mass (Da):20,196
Last modified:July 11, 2006 - v2
Checksum:i4274767A24F2B088
GO

Sequence cautioni

The sequence BAE69057 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008229 Genomic DNA. Translation: BAE69057.1. Different initiation.
RefSeqiWP_024744799.1. NC_007705.1.

Genome annotation databases

EnsemblBacteriaiBAE69057; BAE69057; BAE69057.
GeneIDi3261805.
KEGGixom:XOO2302.
PATRICi24114367. VBIXanOry49434_2606.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008229 Genomic DNA. Translation: BAE69057.1. Different initiation.
RefSeqiWP_024744799.1. NC_007705.1.

3D structure databases

ProteinModelPortaliQ2P320.
SMRiQ2P320.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE69057; BAE69057; BAE69057.
GeneIDi3261805.
KEGGixom:XOO2302.
PATRICi24114367. VBIXanOry49434_2606.

Phylogenomic databases

KOiK00452.
OrthoDBiPOG091H0LPR.

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_XANOM
AccessioniPrimary (citable) accession number: Q2P320
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: November 2, 2016
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.