Q2UB88 (3HAO2_ASPOR) 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 2-1

Gene names

Name:	bna1-2
ORF Names:	AO090102000066

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	179 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.
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	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: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 179	179	3-hydroxyanthranilate 3,4-dioxygenase 2		PRO_0000361982
Sites
	Metal binding	48	1	Iron; catalytic By similarity
	Metal binding	60	1	Iron; catalytic By similarity
	Metal binding	99	1	Iron; catalytic By similarity
	Metal binding	128	1	Divalent metal cation By similarity
	Metal binding	169	1	Divalent metal cation By similarity
	Metal binding	172	1	Divalent metal cation By similarity
	Binding site	44	1	Dioxygen By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	113	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2UB88 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 4F9749F43A058800	FASTA	179	20,762
	10 20 30 40 50 60 MIPPFSFASW VAENEDKLHP PVNNYCLYSG EDFTLMVVGG PNSRNDYHGV FIMVVNQTEE 70 80 90 100 110 120 WFYQVKGDML LRIVENNTTF RDISIKEGEM FLLPGNTPHN PVRFRDTIGL VMERKRPEDS 130 140 150 160 170 LDRLRWYCSK GKHKKPTIIR EEIFHCADLG TQLKPLIERW QIDEESRRCG ACGAIADPK

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007162 Genomic DNA. Translation: BAE61177.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZVF based on UniProtKB P47096.
ProteinModelPortal	Q2UB88.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2UB88.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00009437; CADAORAP00009249; CADAORAG00009437.
GenomeReviews	Gene locus bna1-2 in contig AP007162_GR.
Phylogenomic databases
GeneTree	EFGT00050000005674.
OrthoDB	EOG476P8N.
Family and domain databases
InterPro	IPR010329. 3hydroanth_dOase. IPR011051. Cupin_RmlC_type. IPR014710. RmlC-like_jellyroll. [Graphical view]
Gene3D	G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
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_ASPOR

Accession

Primary (citable) accession number: Q2UB88

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program