B0XVP0 (3HAO2_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-hydroxyanthranilate 3,4-dioxygenase 2
EC=1.13.11.6

Alternative name(s):
3-hydroxyanthranilate oxygenase 2
Short name=3-HAO-2
3-hydroxyanthranilic acid dioxygenase 2
Short name=HAD-2
Biosynthesis of nicotinic acid protein 1-2

Gene names

Name:	bna1-2
ORF Names:	AFUB_033120

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	188 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.
Sequence caution	The sequence EDP55248.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EDP55248.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 188	188	3-hydroxyanthranilate 3,4-dioxygenase 2 HAMAP-Rule MF_03019		PRO_0000361977
Sites
	Metal binding	50	1	Iron; catalytic By similarity
	Metal binding	70	1	Iron; catalytic By similarity
	Metal binding	108	1	Iron; catalytic By similarity
	Binding site	46	1	Dioxygen By similarity
	Binding site	70	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	122	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0XVP0 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 0531413AEF55A832	FASTA	188	22,079
	10 20 30 40 50 60 MATLNPLSWV TWLAENEDKL RPPVNNYCLY QGNDFILMAV GGPNERNDYH VNETEVRLQW 70 80 90 100 110 120 HQPSETNEQE WFYQVQGDML LRVIENDTFR DIPIKEGEMF LLPGNTPHNP VRYKDTIGLV 130 140 150 160 170 180 MERQRPAESR DRLRWYCTKG NHCSPTIIRE EVFHCADLGS QLKPIIERWQ QDEESRRCGE CGCIADPK

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	DS499595 Genomic DNA. Translation: EDP55248.1. Sequence problems.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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

3HAO2_ASPFC

Accession

Primary (citable) accession number: B0XVP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	March 6, 2013
This is version 33 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program