Reviewed, UniProtKB/Swiss-Prot Q4P2Q7 (3HAO_USTMA)

Names and origin

Protein names

Recommended name:
    3-hydroxyanthranilate 3,4-dioxygenase
    EC=1.13.11.6
Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
      Short name=HAD
    3-hydroxyanthranilate oxygenase
      Short name=3-HAO
    Biosynthesis of nicotinic acid protein 1

Gene names

Name:	BNA1
ORF Names:	UM05606

Organism

Ustilago maydis (Smut fungus) [Complete proteome]

Taxonomic identifier

5270 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW
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		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
	Metal binding	124	1	Divalent metal cation By similarity
	Metal binding	167	1	Divalent metal cation By similarity
	Metal binding	170	1	Divalent metal cation 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)
	Q4P2Q7-1 [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: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACP01000203 Genomic DNA. Translation: EAK86472.1.
RefSeq	XP_761753.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q4P2Q7.
Genome annotation databases
GeneID	3633705.
KEGG	uma:UM05606.1.
Phylogenomic databases
OMA	RHSPQRP.
Family and domain databases
InterPro	IPR010329. 3hydroanth_dOase. [Graphical view]
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
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:	November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)