nbaC

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:

no protein annotated in this organism
Kynureninase (kynU), Kynureninase (kynU)
3-hydroxyanthranilate 3,4-dioxygenase (nbaC), 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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	47	DioxygenUniRule annotation	1
Metal bindingⁱ	51	Iron 1; catalyticUniRule annotation	1
Metal bindingⁱ	57	Iron 1; catalyticUniRule annotation	1
Binding siteⁱ	57	SubstrateUniRule annotation	1
Metal bindingⁱ	96	Iron 1; catalyticUniRule annotation	1
Binding siteⁱ	100	SubstrateUniRule annotation	1
Binding siteⁱ	110	SubstrateUniRule annotation	1
Metal bindingⁱ	125	Iron 2UniRule annotation	1
Metal bindingⁱ	128	Iron 2UniRule annotation	1
Metal bindingⁱ	162	Iron 2UniRule annotation	1
Metal bindingⁱ	165	Iron 2UniRule annotation	1

GO - Molecular functionⁱ

3-hydroxyanthranilate 3,4-dioxygenase activity Source: UniProtKB-EC
iron ion binding Source: InterPro

Complete GO annotation...

GO - Biological processⁱ

NAD biosynthetic process Source: UniProtKB-UniPathway

Complete GO annotation...

Keywordsⁱ

Molecular function	Dioxygenase, Oxidoreductase
Biological process	Pyridine nucleotide biosynthesis
Ligand	Iron, Metal-binding

Enzyme and pathway databases

UniPathwayⁱ	UPA00253; UER00330.

UniPathwayⁱ

UPA00253; 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:BALH_1838
Organismⁱ	Bacillus thuringiensis (strain Al Hakam)
Taxonomic identifierⁱ	412694 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus thuringiensis
Proteomesⁱ	UP000000761 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000309575	1 – 179	3-hydroxyanthranilate 3,4-dioxygenaseAdd BLAST		179

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	A0RD64.
SMRⁱ	A0RD64.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

HOGENOMⁱ	HOG000218448.
KEGG Orthology (KO) More...KOⁱ	K00452.
OMAⁱ	NARKDYH.

Family and domain databases

Gene3Dⁱ	2.60.120.10. 1 hit.
HAMAPⁱ	MF_00825. 3_HAO. 1 hit.
InterProⁱ	View protein in InterPro IPR010329. 3hydroanth_dOase. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin.
PANTHERⁱ	PTHR15497. PTHR15497. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06052. 3-HAO. 1 hit.
SUPFAMⁱ	SSF51182. SSF51182. 1 hit.
TIGRFAMsⁱ	TIGR03037. anthran_nbaC. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

A0RD64-1 [UniParc]FASTA Add 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 EEVGEWKCE

Length:179

Mass (Da):20,985

Last modified:January 9, 2007 - v1

Checksum:ⁱ1A5BF15A9B2302AC

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP000485 Genomic DNA. Translation: ABK85157.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_000047734.1. NC_008600.1.

Genome annotation databases

EnsemblBacteriaⁱ	ABK85157; ABK85157; BALH_1838.
KEGGⁱ	btl:BALH_1838.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP000485 Genomic DNA. Translation: ABK85157.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_000047734.1. NC_008600.1.

3D structure databases

ProteinModelPortalⁱ	A0RD64.
SMRⁱ	A0RD64.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	ABK85157; ABK85157; BALH_1838.
KEGGⁱ	btl:BALH_1838.

Phylogenomic databases

HOGENOMⁱ	HOG000218448.
KEGG Orthology (KO) More...KOⁱ	K00452.
OMAⁱ	NARKDYH.

Enzyme and pathway databases

UniPathwayⁱ	UPA00253; UER00330.

UniPathwayⁱ

UPA00253; UER00330.

Family and domain databases

Gene3Dⁱ	2.60.120.10. 1 hit.
HAMAPⁱ	MF_00825. 3_HAO. 1 hit.
InterProⁱ	View protein in InterPro IPR010329. 3hydroanth_dOase. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin.
PANTHERⁱ	PTHR15497. PTHR15497. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06052. 3-HAO. 1 hit.
SUPFAMⁱ	SSF51182. SSF51182. 1 hit.
TIGRFAMsⁱ	TIGR03037. anthran_nbaC. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	3HAO_BACAH
Accessionⁱ	A0RD64Primary (citable) accession number: A0RD64
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
	Last sequence update:	January 9, 2007
	Last modified:	June 7, 2017
	This is version 69 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome

Documents

PATHWAY comments
Index of metabolic and biosynthesis pathways
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.

UniProtKB - A0RD64 (3HAO_BACAH)

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3-hydroxyanthranilate 3,4-dioxygenase

Select a section on the left to see content.

Functionⁱ

Catalytic activityⁱ

Cofactorⁱ

Pathwayⁱ: NAD(+) biosynthesis

Sites

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Enzyme and pathway databases

Names & Taxonomyⁱ

PTM / Processingⁱ

Molecule processing

Structureⁱ

3D structure databases

Family & Domainsⁱ

Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

Sequenceⁱ

Sequence databases

Genome annotation databases

Cross-referencesⁱ

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

Similar proteinsⁱ

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - A0RD64 (3HAO_BACAH)

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3-hydroxyanthranilate 3,4-dioxygenase

nbaC

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: NAD(+) biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: NAD(+) biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ