A1C874 (3HAO2_ASPCL) 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:	ACLA_076350

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	191 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.
Sequence caution	The sequence EAW14595.1 differs from that shown. Reason: Erroneous gene model prediction.

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 – 191	191	3-hydroxyanthranilate 3,4-dioxygenase 2		PRO_0000361975
Sites
	Metal binding	52	1	Iron; catalytic By similarity
	Metal binding	73	1	Iron; catalytic By similarity
	Metal binding	111	1	Iron; catalytic By similarity
	Metal binding	140	1	Divalent metal cation By similarity
	Metal binding	181	1	Divalent metal cation By similarity
	Metal binding	184	1	Divalent metal cation By similarity
	Binding site	48	1	Dioxygen By similarity
	Binding site	73	1	Substrate By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1C874 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: C43A5FC087711AC8	FASTA	191	22,148
	10 20 30 40 50 60 MNPMPLSPLF FATWLAENED QLRPPVNNYC LYQGNDFILM AVGGPNERND YHVNETEVCL 70 80 90 100 110 120 QPSWCSREAN EQEWFYQVKG DMLLRVVENN AFRDIPIKEG EMFLLPGNTP HNPVRFKDTI 130 140 150 160 170 180 GLVMERQRPA GSRDRLRWYC TKGDHASPTI IREEVFHCSD LGTQLKPIIE QWQQDEDGRR 190 CAECSCIADP K

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: 18404212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027045 Genomic DNA. Translation: EAW14595.1. Sequence problems.
RefSeq	XP_001276021.1. XM_001276020.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A1C874.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4708052.
KEGG	act:ACLA_076350.
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.
KO	K00452.
PANTHER	PTHR15497. PTHR15497. 1 hit.
Pfam	PF06052. 3-HAO. 2 hits. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO2_ASPCL

Accession

Primary (citable) accession number: A1C874

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	November 16, 2011
This is version 35 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program