Reviewed, UniProtKB/Swiss-Prot A5E0Z9 (3HAO_LODEL)

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:	LELG_03286

Organism

Lodderomyces elongisporus (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

36914 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	175 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 – 175	175	3-hydroxyanthranilate 3,4-dioxygenase		PRO_0000361988
Sites
	Metal binding	49	1	Iron; catalytic By similarity
	Metal binding	55	1	Iron; catalytic By similarity
	Metal binding	93	1	Iron; catalytic By similarity
	Metal binding	122	1	Divalent metal cation By similarity
	Metal binding	125	1	Divalent metal cation By similarity
	Metal binding	159	1	Divalent metal cation By similarity
	Metal binding	162	1	Divalent metal cation By similarity
	Binding site	45	1	Dioxygen By similarity
	Binding site	55	1	Substrate By similarity
	Binding site	97	1	Substrate By similarity
	Binding site	107	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5E0Z9-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 6ABC58FEBA0680A1	FASTA	175	20,157
	10 20 30 40 50 60 MPLPEPLNIK AWVEENEHLL KPPVNNFCLH RGGFTVMIVG GPNERSDYHI NQTPEYFYQY 70 80 90 100 110 120 KGTMCLKVVD EGKFRDIYIR EGDTFLLPPN VPHNPCRFEN TVGIVVEQDR PKGVNDRIRW 130 140 150 160 170 YCARCESIVC EEEFYLTDLG TQIKDAIVAF DSNIEAKTCK NCGHVNSSKR EPAEF

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 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH981527 Genomic DNA. Translation: EDK45107.1.
RefSeq	XP_001525358.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5232567.
Phylogenomic databases
OMA	RHSPQRP.
Family and domain databases
InterPro	IPR010329. 3hydroanth_dOase. IPR014710. RmlC-like_jellyroll. [Graphical view]
Gene3D	G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO_LODEL

Accession

Primary (citable) accession number: A5E0Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	June 12, 2007
Last modified:	November 3, 2009
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)