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Q4WCF1 (3HAO1_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-hydroxyanthranilate 3,4-dioxygenase 1
EC=1.13.11.6
Alternative name(s):
3-hydroxyanthranilate oxygenase 1
Short name=3-HAO-1
3-hydroxyanthranilic acid dioxygenase 1
Short name=HAD-1
Biosynthesis of nicotinic acid protein 1-1
Gene names
Name:bna1-1
ORF Names:AFUA_8G04650
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceInferred 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 processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpyridine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1921923-hydroxyanthranilate 3,4-dioxygenase 1
PRO_0000361978

Sites

Metal binding541Iron; catalytic By similarity
Metal binding601Iron; catalytic By similarity
Metal binding1021Iron; catalytic By similarity
Metal binding1311Divalent metal cation By similarity
Metal binding1341Divalent metal cation By similarity
Metal binding1681Divalent metal cation By similarity
Metal binding1711Divalent metal cation By similarity
Binding site501Dioxygen By similarity
Binding site601Substrate By similarity
Binding site1061Substrate By similarity
Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WCF1 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 148D406C365727F7

FASTA19221,705
        10         20         30         40         50         60 
MLPPALNIPK WLEENSHLLQ PPVNNYCVYH PSSPATAGYT VMIVGGPNAR TDYHINTTPE 

        70         80         90        100        110        120 
FFYQYRGSML LKTVDTSVSP PVFQDIPIHE GSIFLLPANT PHCPVRFKDT VGVVMEQPRP 

       130        140        150        160        170        180 
KDAVDTMLWF CKKCGEVVWE KRFVCTDLGT QVKEVVEEFA ADQEKRTCKA CGTIAETRYQ 

       190 
EGEVVQPPRF LE

« Hide

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. expand/collapse author list , 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: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AAHF01000013 Genomic DNA. Translation: EAL85233.1.
RefSeqXP_747271.1. XM_742178.1.

3D structure databases

HSSPHSSP built from PDB template 1ZVF based on UniProtKB P47096.
ProteinModelPortalQ4WCF1.
SMRQ4WCF1. Positions 5-180.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4WCF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00003260; CADAFUAP00003260; CADAFUAG00003260.
GeneID3504643.
GenomeReviewsGene locus bna1-1 in contig CM000176_GR.
KEGGafm:AFUA_8G04650.

Phylogenomic databases

eggNOGfuNOG08759.
GeneTreeEFGT00050000005674.
HOGENOMHBG341987.
OMALKPPVNN.
OrthoDBEOG476P8N.

Family and domain databases

InterProIPR010329. 3hydroanth_dOase.
IPR011051. Cupin_RmlC_type.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
KOK00452.
PANTHERPTHR15497. PTHR15497. 1 hit.
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
SUPFAMSSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMsTIGR03037. Anthran_nbaC. 1 hit.
ProtoNetSearch...

Entry information

Entry name3HAO1_ASPFU
AccessionPrimary (citable) accession number: Q4WCF1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 5, 2005
Last modified: December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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