Reviewed, UniProtKB/Swiss-Prot Q5KLD9 (3HAO_CRYNE)

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:	CNB05620, CNBB0170

Organism

Cryptococcus neoformans (Filobasidiella neoformans) [Complete proteome]

Taxonomic identifier

5207 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length	176 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 – 176	176	3-hydroxyanthranilate 3,4-dioxygenase		PRO_0000361987
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	127	1	Divalent metal cation By similarity
	Metal binding	166	1	Divalent metal cation By similarity
	Metal binding	169	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)
	Q5KLD9-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: C3932D0010B21B6C	FASTA	176	20,198
	10 20 30 40 50 60 MLPPPINFPK WLEANSHLLK PPVGNKCLYK GSNFITMIVG GPNTRVDFHI NTTEEWFYQY 70 80 90 100 110 120 KGAMTLKVVD EGKIKDIVIE EGDMFLLPAN TPHSPRRVAD TIGVVMEMVR PGEFLDTMRW 130 140 150 160 170 YCPSPTHANA EKLVTIREVT FYCSDLDTQL KPVIERWMSD EEWRRCPECG EVAPPK

References

[1]

"The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans." Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S. , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W. Science 307:1321-1324(2005) [PubMed: 15653466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B-3501A and JEC21.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017342 Genomic DNA. Translation: AAW41998.1. AAEY01000006 Genomic DNA. Translation: EAL22796.1.
RefSeq	XP_569305.1. XP_777443.1.
UniGene	Fne.1958
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5KLD9.
Genome annotation databases
GeneID	3255579. 4934109.
GenomeReviews	Gene locus CNB05620 in contig AE017342_GR. Gene locus CNBB0170 in contig CM000041_GR.
KEGG	cnb:CNBB0170. cne:CNB05620.
Phylogenomic databases
HOGENOM	Q5KLD9.
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_CRYNE

Accession

Primary (citable) accession number: Q5KLD9
Secondary accession number(s): Q55YJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 15, 2005
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)