Q4P2Q7 (3HAO_USTMA) 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:	UM05606

Organism

Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]

Taxonomic identifier

237631 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago › Ustilago maydis

Protein attributes

Sequence length	181 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 Reference 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 – 181	181	3-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019		PRO_0000361995
Sites
	Metal binding	50	1	Iron; catalytic By similarity
	Metal binding	56	1	Iron; catalytic By similarity
	Metal binding	95	1	Iron; catalytic By similarity
	Binding site	46	1	Dioxygen By similarity
	Binding site	56	1	Substrate By similarity
	Binding site	99	1	Substrate By similarity
	Binding site	109	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4P2Q7 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 75124AC34209CF79	FASTA	181	20,640
	10 20 30 40 50 60 MPFPLPLNFP KWLSENEHLL QPPVGNFCLF RTRDYTVMAV GGPNARSDYH YQPTEEFFYQ 70 80 90 100 110 120 YKGDMLLKVI DEDGKFQDIP IKQGEMFMLP AHTPHSPVRF ANTVGIVVER TRPDGSPDAM 130 140 150 160 170 180 RWYCPNKEAH GETPTLVKEV HFQCTDLGTQ LKPIIDAWVN DEAGRQCSHC GYTQGARELP A

References

[1]

"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W. Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521 / FGSC 9021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACP01000203 Genomic DNA. Translation: EAK86472.1.
RefSeq	XP_761753.1. XM_756660.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZVF based on UniProtKB P47096.
ProteinModelPortal	Q4P2Q7.
SMR	Q4P2Q7. Positions 3-177.
ModBase	Search...
Protein-protein interaction databases
STRING	5270.UM05606.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	UM05606T0; UM05606P0; UM05606.
GeneID	3633705.
KEGG	uma:UM05606.1.
Phylogenomic databases
eggNOG	NOG77058.
KO	K00452.
OMA	HSPQRPE.
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_USTMA

Accession

Primary (citable) accession number: Q4P2Q7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	July 19, 2005
Last modified:	April 3, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program