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Protein

Kynurenine formamidase

Gene

BNA7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.UniRule annotation1 Publication

Catalytic activityi

N-formyl-L-kynurenine + H2O = formate + L-kynurenine.UniRule annotation1 Publication

Pathwayi: L-tryptophan degradation via kynurenine pathway

This protein is involved in step 2 of the subpathway that synthesizes L-kynurenine from L-tryptophan.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Kynurenine formamidase (BNA7)
This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei110NucleophileUniRule annotation1
Active sitei211UniRule annotation1
Active sitei243UniRule annotation1

GO - Molecular functioni

  • arylformamidase activity Source: SGD

GO - Biological processi

  • 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  • NAD biosynthetic process Source: SGD
  • positive regulation of cell growth Source: UniProtKB
  • tryptophan catabolic process to kynurenine Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Tryptophan catabolism

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-17.
BRENDAi3.5.1.9. 984.
UniPathwayiUPA00333; UER00454.

Protein family/group databases

ESTHERiyeast-YDR428C. Kynurenine-formamidase.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynurenine formamidaseUniRule annotation (EC:3.5.1.9UniRule annotation)
Short name:
KFAUniRule annotation
Short name:
KFaseUniRule annotation
Alternative name(s):
ArylformamidaseUniRule annotation
Biosynthesis of nicotinic acid protein 7
N-formylkynurenine formamidaseUniRule annotation
Short name:
FKFUniRule annotation
Gene namesi
Name:BNA7UniRule annotation
Ordered Locus Names:YDR428C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR428C.
SGDiS000002836. BNA7.

Pathology & Biotechi

Disruption phenotypei

Cells exhibit slow growth in the absence of nicotinate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002346601 – 261Kynurenine formamidaseAdd BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04066.
PRIDEiQ04066.

PTM databases

iPTMnetiQ04066.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

BioGridi32486. 8 interactors.
DIPiDIP-4139N.
IntActiQ04066. 1 interactor.
MINTiMINT-555667.

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 17Combined sources3
Beta strandi19 – 22Combined sources4
Beta strandi30 – 35Combined sources6
Turni39 – 41Combined sources3
Helixi47 – 50Combined sources4
Helixi51 – 60Combined sources10
Beta strandi66 – 71Combined sources6
Turni76 – 78Combined sources3
Helixi83 – 99Combined sources17
Beta strandi104 – 109Combined sources6
Helixi111 – 120Combined sources10
Helixi121 – 124Combined sources4
Turni127 – 129Combined sources3
Helixi132 – 141Combined sources10
Beta strandi144 – 151Combined sources8
Helixi156 – 162Combined sources7
Helixi164 – 166Combined sources3
Helixi167 – 173Combined sources7
Helixi178 – 180Combined sources3
Helixi185 – 199Combined sources15
Beta strandi202 – 208Combined sources7
Helixi217 – 228Combined sources12
Beta strandi233 – 238Combined sources6
Helixi243 – 248Combined sources6
Helixi250 – 258Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VKHX-ray1.85A/B1-261[»]
ProteinModelPortaliQ04066.
SMRiQ04066.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04066.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi36 – 40HGGXW5

Domaini

The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.1 Publication

Sequence similaritiesi

Belongs to the kynurenine formamidase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000065929.
InParanoidiQ04066.
KOiK14263.
OMAiEHEQVYR.
OrthoDBiEOG092C48GX.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_03014. KFase. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR027519. KFase_ver/fungi-typ.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q04066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNTVRAISP DITLFNKTLT FQEISQNTRE AVIYIHGGAW NDPENTPNDF
60 70 80 90 100
NQLANTIKSM DTESTVCQYS IEYRLSPEIT NPRNLYDAVS NITRLVKEKG
110 120 130 140 150
LTNINMVGHS VGATFIWQIL AALKDPQEKM SEAQLQMLGL LQIVKRVFLL
160 170 180 190 200
DGIYSLKELL VEYPEYDCFT RLAFPDGIQM YEEEPSRVMP YVKKALSRFS
210 220 230 240 250
IDMHLVHSYS DELLTLRQTN CLISCLQDYQ LSFKLYLDDL GLHNDVYKNG
260
KVAKYIFDNI C
Length:261
Mass (Da):29,991
Last modified:November 1, 1996 - v1
Checksum:iF07FE52DD9D2EF92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64885.1.
BK006938 Genomic DNA. Translation: DAA12267.1.
PIRiS69709.
RefSeqiNP_010716.3. NM_001180736.3.

Genome annotation databases

EnsemblFungiiYDR428C; YDR428C; YDR428C.
GeneIDi852038.
KEGGisce:YDR428C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64885.1.
BK006938 Genomic DNA. Translation: DAA12267.1.
PIRiS69709.
RefSeqiNP_010716.3. NM_001180736.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VKHX-ray1.85A/B1-261[»]
ProteinModelPortaliQ04066.
SMRiQ04066.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32486. 8 interactors.
DIPiDIP-4139N.
IntActiQ04066. 1 interactor.
MINTiMINT-555667.

Protein family/group databases

ESTHERiyeast-YDR428C. Kynurenine-formamidase.

PTM databases

iPTMnetiQ04066.

Proteomic databases

MaxQBiQ04066.
PRIDEiQ04066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR428C; YDR428C; YDR428C.
GeneIDi852038.
KEGGisce:YDR428C.

Organism-specific databases

EuPathDBiFungiDB:YDR428C.
SGDiS000002836. BNA7.

Phylogenomic databases

HOGENOMiHOG000065929.
InParanoidiQ04066.
KOiK14263.
OMAiEHEQVYR.
OrthoDBiEOG092C48GX.

Enzyme and pathway databases

UniPathwayiUPA00333; UER00454.
BioCyciYEAST:MONOMER3O-17.
BRENDAi3.5.1.9. 984.

Miscellaneous databases

EvolutionaryTraceiQ04066.
PROiQ04066.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_03014. KFase. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR027519. KFase_ver/fungi-typ.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKFA_YEAST
AccessioniPrimary (citable) accession number: Q04066
Secondary accession number(s): D6VT57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.