Reviewed, UniProtKB/Swiss-Prot Q4WZC3 (3HAO2_ASPFU)

Names and origin

Protein names

Recommended name:
    3-hydroxyanthranilate 3,4-dioxygenase 2
    EC=1.13.11.6
Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase 2
      Short name=HAD-2
    3-hydroxyanthranilate oxygenase 2
      Short name=3-HAO-2
    Biosynthesis of nicotinic acid protein 1-2

Gene names

Name:	bna1-2
ORF Names:	AFUA_2G17450

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	188 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.
Sequence caution	The sequence EAL94042.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAL94042.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 188	188	3-hydroxyanthranilate 3,4-dioxygenase 2		PRO_0000361979
Sites
	Metal binding	50	1	Iron; catalytic By similarity
	Metal binding	70	1	Iron; catalytic By similarity
	Metal binding	108	1	Iron; catalytic By similarity
	Metal binding	137	1	Divalent metal cation By similarity
	Metal binding	143	1	Divalent metal cation By similarity
	Metal binding	178	1	Divalent metal cation By similarity
	Metal binding	181	1	Divalent metal cation By similarity
	Binding site	46	1	Dioxygen By similarity
	Binding site	70	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity
	Binding site	122	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4WZC3-1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 0531413AEF55A832	FASTA	188	22,079
	10 20 30 40 50 60 MATLNPLSWV TWLAENEDKL RPPVNNYCLY QGNDFILMAV GGPNERNDYH VNETEVRLQW 70 80 90 100 110 120 HQPSETNEQE WFYQVQGDML LRVIENDTFR DIPIKEGEMF LLPGNTPHNP VRYKDTIGLV 130 140 150 160 170 180 MERQRPAESR DRLRWYCTKG NHCSPTIIRE EVFHCADLGS QLKPIIERWQ QDEESRRCGE CGCIADPK

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAHF01000001 Genomic DNA. Translation: EAL94042.1. Sequence problems.
RefSeq	XP_756080.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q4WZC3.
Genome annotation databases
GeneID	3513434.
GenomeReviews	Gene locus bna1-2 in contig CM000170_GR.
KEGG	afm:AFUA_2G17450.
Phylogenomic databases
HOGENOM	Q4WZC3.
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

3HAO2_ASPFU

Accession

Primary (citable) accession number: Q4WZC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	September 22, 2009
This is version 33 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)