Reviewed, UniProtKB/Swiss-Prot Q6CFX1 (3HAO_YARLI)

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
Ordered Locus Names:	YALI0B02852g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	171 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 – 171	171	3-hydroxyanthranilate 3,4-dioxygenase		PRO_0000361996
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	126	1	Divalent metal cation By similarity
	Metal binding	160	1	Divalent metal cation By similarity
	Metal binding	163	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)
	Q6CFX1-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: B181F188D026A2AD	FASTA	171	19,550
	10 20 30 40 50 60 MLQEPINLPK WLEENQHLLK PPVNNFCIQR GGYTVMIVGG PNARTDYHIN QTPEWFHQKK 70 80 90 100 110 120 GHMTLKVVDD GEFRDITINE GDIFLLPANV PHNPVRYADT IGVVVEQDRP EGMKDALRWY 130 140 150 160 170 CPNEKCREIV FENSFQLVDL GTQIKEAILD FDGDIEKRTC KACGTVATSR P

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382128 Genomic DNA. Translation: CAG82659.1.
RefSeq	XP_500441.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6CFX1.
Genome annotation databases
GeneID	2907509.
GenomeReviews	Gene locus YALI0B02852g in contig CR382128_GR.
KEGG	yli:YALI0B02852g.
Phylogenomic databases
HOGENOM	Q6CFX1.
OMA	RHSPQRP.
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_YARLI

Accession

Primary (citable) accession number: Q6CFX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)