A0RD64 (3HAO_BACAH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-hydroxyanthranilate 3,4-dioxygenase
EC=1.13.11.6

Alternative name(s):
3-hydroxyanthranilate oxygenase
Short name=3-HAO
3-hydroxyanthranilic acid dioxygenase
Short name=HAD

Gene names

Name:	nbaC
Ordered Locus Names:	BALH_1838

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus thuringiensis

Protein attributes

Sequence length	179 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate By similarity. HAMAP-Rule MF_00825
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP-Rule MF_00825
Cofactor	Binds 2 Fe2+ ions per subunit By similarity. HAMAP-Rule MF_00825
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_00825
Sequence similarities	Belongs to the 3-HAO family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	'de novo' NAD biosynthetic process from tryptophan Inferred from electronic annotation. Source: UniProtKB-HAMAP anthranilate metabolic process Inferred from electronic annotation. Source: UniProtKB-HAMAP quinolinate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-HAMAP tryptophan catabolic process Inferred from electronic annotation. Source: UniProtKB-HAMAP
Molecular_function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP ferrous iron binding Inferred from electronic annotation. Source: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 179	179	3-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_00825		PRO_0000309575
Sites
	Metal binding	51	1	Iron 1; catalytic By similarity
	Metal binding	57	1	Iron 1; catalytic By similarity
	Metal binding	96	1	Iron 1; catalytic By similarity
	Metal binding	125	1	Iron 2 By similarity
	Metal binding	128	1	Iron 2 By similarity
	Metal binding	162	1	Iron 2 By similarity
	Metal binding	165	1	Iron 2 By similarity
	Binding site	47	1	Dioxygen By similarity
	Binding site	57	1	Substrate By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	110	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0RD64 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 1A5BF15A9B2302AC	FASTA	179	20,985
	10 20 30 40 50 60 MSKTLQSFNL LKWIDENKEL LKPPVNNKVI WQDSEFIAMI LGGPNRRRDF HVDPSDEFFY 70 80 90 100 110 120 QIKGECYVEC ITEEGKREVV TVKEGDVFML PAMVPHSPHR VANTYGLVIE RKRSQGELED 130 140 150 160 170 FVWFCDECNH EMHRVRVQLS DIEKQVKEAI HSFNSNKEIR ACKNCGHIMP EEVGEWKCE

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Al Hakam.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000485 Genomic DNA. Translation: ABK85157.1.
RefSeq	YP_894664.1. NC_008600.1.
3D structure databases
ProteinModelPortal	A0RD64.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	412694.BALH_1838.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK85157; ABK85157; BALH_1838.
GeneID	4545488.
KEGG	btl:BALH_1838.
PATRIC	18996130. VBIBacThu63319_2067.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	NOG77058.
HOGENOM	HOG000218448.
KO	K00452.
OMA	HINQTPE.
OrthoDB	EOG6PW234.
ProtClustDB	PRK13264.
Enzyme and pathway databases
BioCyc	BTHU412694:GH1W-1849-MONOMER.
UniPathway	UPA00253; UER00330.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
HAMAP	MF_00825. 3_HAO.
InterPro	IPR010329. 3hydroanth_dOase. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR15497. PTHR15497. 1 hit.
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
SUPFAM	SSF51182. SSF51182. 1 hit.
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO_BACAH

Accession

Primary (citable) accession number: A0RD64

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	January 9, 2007
Last modified:	February 19, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program