B0Y9Z9 (3HAO1_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-hydroxyanthranilate 3,4-dioxygenase 1
EC=1.13.11.6

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

Gene names

Name:	bna1-1
ORF Names:	AFUB_082850

Organism

Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]

Taxonomic identifier

451804 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Neosartorya fumigata

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_03019
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP-Rule MF_03019
Cofactor	Fe2+ ion By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_03019
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	de novo NAD biosynthetic process from tryptophan Inferred from electronic annotation. Source: EnsemblFungi
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: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 192	192	3-hydroxyanthranilate 3,4-dioxygenase 1 HAMAP-Rule MF_03019		PRO_0000361976
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	134	1	Divalent metal cation By similarity
	Metal binding	168	1	Divalent metal cation By similarity
	Metal binding	171	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)
	B0Y9Z9 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: 148D406C365727F7	FASTA	192	21,705
	10 20 30 40 50 60 MLPPALNIPK WLEENSHLLQ PPVNNYCVYH PSSPATAGYT VMIVGGPNAR TDYHINTTPE 70 80 90 100 110 120 FFYQYRGSML LKTVDTSVSP PVFQDIPIHE GSIFLLPANT PHCPVRFKDT VGVVMEQPRP 130 140 150 160 170 180 KDAVDTMLWF CKKCGEVVWE KRFVCTDLGT QVKEVVEEFA ADQEKRTCKA CGTIAETRYQ 190 EGEVVQPPRF LE

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CEA10 / CBS 144.89 / FGSC A1163.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS499600 Genomic DNA. Translation: EDP48842.1.
3D structure databases
ProteinModelPortal	B0Y9Z9.
SMR	B0Y9Z9. Positions 5-180.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUBT00008214; CADAFUBP00008068; CADAFUBG00008214.
Phylogenomic databases
HOGENOM	HOG000218448.
Enzyme and pathway databases
UniPathway	UPA00253; UER00330.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
HAMAP	MF_00825. 3_HAO.
InterPro	IPR010329. 3hydroanth_dOase. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR15497. PTHR15497. 1 hit.
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR03037. anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO1_ASPFC

Accession

Primary (citable) accession number: B0Y9Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	April 8, 2008
Last modified:	March 6, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program