A4REV8 (3HAO_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	BNA1
ORF Names:	MGG_00549

Organism

Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) [Complete proteome]

Taxonomic identifier

242507 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe › Magnaporthe oryzae

Protein attributes

Sequence length	184 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 – 184	184	3-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019		PRO_0000361989
Sites
	Metal binding	48	1	Iron; catalytic By similarity
	Metal binding	54	1	Iron; catalytic By similarity
	Metal binding	92	1	Iron; catalytic By similarity
	Metal binding	121	1	Divalent metal cation By similarity
	Metal binding	126	1	Divalent metal cation By similarity
	Metal binding	162	1	Divalent metal cation By similarity
	Metal binding	165	1	Divalent metal cation By similarity
	Binding site	44	1	Dioxygen By similarity
	Binding site	54	1	Substrate By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	106	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4REV8 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 0E3F049B9F8B3A4D	FASTA	184	20,798
	10 20 30 40 50 60 MLGPPVNLPK WLEENSHLLK PPINNYCVYN DDFTVMIVGG PNARTDYHIN QTPEWFYQYK 70 80 90 100 110 120 GAMMLKVVDD GVFRDIIIRE GDMFLLPGNT PHNPVRFADT VGVVLEQRRP EGSIDRMRWY 130 140 150 160 170 180 CQNPDCTPGQ VVHEASFHCT DLGTQIKAGV ESFKTDESLR KCGKCGELAD WCPKPGSILD PNKA

References

[1]

"The genome sequence of the rice blast fungus Magnaporthe grisea." Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M. , Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W. Nature 434:980-986(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 70-15 / ATCC MYA-4617 / FGSC 8958.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM001235 Genomic DNA. Translation: EHA48917.1.
RefSeq	XP_003718501.1. XM_003718453.1.
3D structure databases
ProteinModelPortal	A4REV8.
SMR	A4REV8. Positions 5-168.
ModBase	Search...
Protein-protein interaction databases
STRING	148305.A4REV8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	MGG_00549T0; MGG_00549T0; MGG_00549.
GeneID	2674643.
KEGG	mgr:MGG_00549.
Phylogenomic databases
eggNOG	NOG77058.
KO	K00452.
OrthoDB	EOG476P8N.
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

3HAO_MAGO7

Accession

Primary (citable) accession number: A4REV8
Secondary accession number(s): G4NBG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	May 15, 2007
Last modified:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program