Reviewed, UniProtKB/Swiss-Prot A5DLW3 (3HAO_PICGU)

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:	PGUG_04264

Organism

Pichia guilliermondii (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

4929 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

Protein attributes

Sequence length	169 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 – 169	169	3-hydroxyanthranilate 3,4-dioxygenase		PRO_0000361992
Sites
	Metal binding	48	1	Iron; catalytic By similarity
	Metal binding	54	1	Iron; catalytic By similarity
	Metal binding	92	1	Iron; catalytic By similarity
	Metal binding	121	1	Divalent metal cation By similarity
	Metal binding	124	1	Divalent metal cation By similarity
	Metal binding	158	1	Divalent metal cation By similarity
	Metal binding	160	1	Divalent metal cation By similarity
	Binding site	44	1	Dioxygen By similarity
	Binding site	54	1	Substrate By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	106	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5DLW3-1 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: 8E7F890431BA2F0A	FASTA	169	19,284
	10 20 30 40 50 60 MLAEPINLQS WISENKDLLQ PPVNNYCLHR GGATVMIVGG PNERTDYHVN QTPEYFHQIK 70 80 90 100 110 120 GDMTLKVVDD GKFRDITIRE GDSFLLPGNV PHNPVRYADT IGLVVEQDRP KGVNDKIRWY 130 140 150 160 CSNCREIVHQ VEFYCYDLGT QVKDAILAFD GDDEARTCKC GTYNYSRPN

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH408159 Genomic DNA. Translation: EDK40166.2.
3D structure databases
ModBase	Search...
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_PICGU

Accession

Primary (citable) accession number: A5DLW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	July 22, 2008
Last modified:	October 13, 2009
This is version 14 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)