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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Bacillus cereus (strain 03BB102)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471DioxygenUniRule annotation
Metal bindingi51 – 511Iron 1; catalyticUniRule annotation
Metal bindingi57 – 571Iron 1; catalyticUniRule annotation
Binding sitei57 – 571SubstrateUniRule annotation
Metal bindingi96 – 961Iron 1; catalyticUniRule annotation
Binding sitei100 – 1001SubstrateUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Metal bindingi125 – 1251Iron 2UniRule annotation
Metal bindingi128 – 1281Iron 2UniRule annotation
Metal bindingi162 – 1621Iron 2UniRule annotation
Metal bindingi165 – 1651Iron 2UniRule annotation

GO - Molecular functioni

  1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: UniProtKB-HAMAP
  2. ferrous iron binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  4. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciBCER572264:GH22-2106-MONOMER.
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:BCA_2149
OrganismiBacillus cereus (strain 03BB102)
Taxonomic identifieri572264 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002210: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1791793-hydroxyanthranilate 3,4-dioxygenasePRO_1000148766Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi572264.BCA_2149.

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG6PW234.

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.

C1ERL1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKTLQSFNL LKWIDENKEL LKPPVNNKVI WQDSEFIAMI LGGPNRRRDF
60 70 80 90 100
HVDPSDEFFY QIKGECYVEC ITEEGKREVV TVKEGDVFML PAMVPHSPHR
110 120 130 140 150
VANTYGLVIE RKRSQGELED FVWFCDECNH EMHRVRVQLS DIEKQVKEAI
160 170
HSFNSNKEIR ACKNCGHIMP EEVEEWKCE
Length:179
Mass (Da):21,057
Last modified:May 26, 2009 - v1
Checksum:i1A5BF15A9B2062AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001407 Genomic DNA. Translation: ACO28730.1.
RefSeqiYP_002749423.1. NC_012472.1.

Genome annotation databases

EnsemblBacteriaiACO28730; ACO28730; BCA_2149.
GeneIDi7691240.
KEGGibcx:BCA_2149.
PATRICi18817419. VBIBacCer84800_2026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001407 Genomic DNA. Translation: ACO28730.1.
RefSeqiYP_002749423.1. NC_012472.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi572264.BCA_2149.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACO28730; ACO28730; BCA_2149.
GeneIDi7691240.
KEGGibcx:BCA_2149.
PATRICi18817419. VBIBacCer84800_2026.

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG6PW234.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.
BioCyciBCER572264:GH22-2106-MONOMER.

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

  1. "Genome sequence of Bacillus cereus 03BB102."
    Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C., Sutton G., Sims D.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 03BB102.

Entry informationi

Entry namei3HAO_BACC3
AccessioniPrimary (citable) accession number: C1ERL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: January 7, 2015
This is version 42 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

Complete 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.