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A7TJ85 (BNA7_VANPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 25. 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:
Probable kynurenine formamidase

EC=3.5.1.9
Alternative name(s):
Biosynthesis of nicotinic acid protein 7
Probable N-formylkynurenine formamidase
Gene names
Name:BNA7
ORF Names:Kpol_1004p28
OrganismVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]
Taxonomic identifier436907 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeVanderwaltozyma

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H) By similarity.

Catalytic activity

N-formyl-L-kynurenine + H2O = formate + L-kynurenine.

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.

Sequence similarities

Belongs to the BNA7 family.

Ontologies

Keywords
   Biological processTryptophan catabolism
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtryptophan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionarylformamidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Probable kynurenine formamidase
PRO_0000361885

Sites

Active site331 Potential
Active site1121 Potential

Sequences

Sequence LengthMass (Da)Tools
A7TJ85 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 222B0368A9D94B99

FASTA26130,049
        10         20         30         40         50         60 
MNDPTDTLYH QTAIHKLAEI GKNCKHLGII FIHGGAWVDP LNTSNDFKGI AGEISKVIEN 

        70         80         90        100        110        120 
NNTQGFNISM FGIEYRLSPS VKHPIHITDV ITNTYKLINE YKIDILYIVG HSVGATLGLQ 

       130        140        150        160        170        180 
LATDNRDYLI KYSSQLHLIR STIQGLFLLD GIYSLQELLK EYPTYDSFIS KAFTNYELEF 

       190        200        210        220        230        240 
QDPKEYLDKE QQFIKNLSFY IIHSFQDELL TLRQTDYLVE LLKAKEISFN LSISDYGRHN 

       250        260 
DVYINDRVAK LIIFNILSNI N 

« Hide

References

[1]"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed: 17494770] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 22028 / DSM 70294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS480400 Genomic DNA. Translation: EDO17654.1.
RefSeqXP_001645512.1. XM_001645462.1.

3D structure databases

ProteinModelPortalA7TJ85.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5545893.
KEGGvpo:Kpol_1004p28.

Phylogenomic databases

OrthoDBEOG4GMZ6M.
PhylomeDBA7TJ85.

Family and domain databases

InterProIPR013094. AB_hydrolase_3.
[Graphical view]
KOK14263.
PfamPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBNA7_VANPO
AccessionPrimary (citable) accession number: A7TJ85
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: October 2, 2007
Last modified: December 14, 2011
This is version 25 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