Reviewed, UniProtKB/Swiss-Prot A2R8S7 (3HAO_ASPNC)

Names and origin

Protein names

Recommended name:
    3-hydroxyanthranilate 3,4-dioxygenase
    EC=1.13.11.6
Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
      Short name=HAD
    3-hydroxyanthranilate oxygenase
      Short name=3-HAO
    Biosynthesis of nicotinic acid protein 1

Gene names

Name:	bna1
ORF Names:	An16g08210

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.
Cofactor	Fe2+ ion By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the 3-HAO family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 189	189	3-hydroxyanthranilate 3,4-dioxygenase		PRO_0000361980
Sites
	Metal binding	54	1	Iron; catalytic By similarity
	Metal binding	60	1	Iron; catalytic By similarity
	Metal binding	102	1	Iron; catalytic By similarity
	Metal binding	131	1	Divalent metal cation By similarity
	Metal binding	136	1	Divalent metal cation By similarity
	Metal binding	170	1	Divalent metal cation By similarity
	Metal binding	173	1	Divalent metal cation By similarity
	Binding site	50	1	Dioxygen By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	116	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2R8S7-1 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: F10A9D82A81A07A9	FASTA	189	21,338
	10 20 30 40 50 60 MLPPALNIPK WLETNSHLLQ PPVNNYCVYH PSSPATQGYT VMIVGGPNAR TDYHINTTPE 70 80 90 100 110 120 FFYQYKGSML LRTVDESSTP PTFQDIPIHE GSLFLLPANT PHCPVRFKDT VGVVMEQPRK 130 140 150 160 170 180 EGAVDAMRWY CRNKDCGKVV WEKRFVCTDL GTQVKQVVEE FAGDEEKRTC KACGVVARSK YEEGEVVQP

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed: 17259976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM270377 Genomic DNA. Translation: CAK47070.1.
RefSeq	XP_001398119.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4989212.
GenomeReviews	Gene locus bna1 in contig AM270995_GR.
KEGG	ang:An16g08210.
Family and domain databases
InterPro	IPR010329. 3hydroanth_dOase. [Graphical view]
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO_ASPNC

Accession

Primary (citable) accession number: A2R8S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	March 6, 2007
Last modified:	September 22, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)