Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101NucleophileUniRule annotation
Active sitei211 – 2111UniRule annotation
Active sitei243 – 2431UniRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Kynurenine formamidasePRO_0000234660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04066.

PTM databases

iPTMnetiQ04066.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

BioGridi32486. 8 interactions.
DIPiDIP-4139N.
IntActiQ04066. 1 interaction.
MINTiMINT-555667.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 173Combined sources
Beta strandi19 – 224Combined sources
Beta strandi30 – 356Combined sources
Turni39 – 413Combined sources
Helixi47 – 504Combined sources
Helixi51 – 6010Combined sources
Beta strandi66 – 716Combined sources
Turni76 – 783Combined sources
Helixi83 – 9917Combined sources
Beta strandi104 – 1096Combined sources
Helixi111 – 12010Combined sources
Helixi121 – 1244Combined sources
Turni127 – 1293Combined sources
Helixi132 – 14110Combined sources
Beta strandi144 – 1518Combined sources
Helixi156 – 1627Combined sources
Helixi164 – 1663Combined sources
Helixi167 – 1737Combined sources
Helixi178 – 1803Combined sources
Helixi185 – 19915Combined sources
Beta strandi202 – 2087Combined sources
Helixi217 – 22812Combined sources
Beta strandi233 – 2386Combined sources
Helixi243 – 2486Combined sources
Helixi250 – 2589Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VKHX-ray1.85A/B1-261[»]
ProteinModelPortaliQ04066.
SMRiQ04066. Positions 4-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04066.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 405HGGXW

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.
OrthoDBiEOG7NSBCS.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_03014. KFase.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1VKHX-ray1.85A/B1-261[»]
ProteinModelPortaliQ04066.
SMRiQ04066. Positions 4-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32486. 8 interactions.
DIPiDIP-4139N.
IntActiQ04066. 1 interaction.
MINTiMINT-555667.

Protein family/group databases

ESTHERiyeast-YDR428C. Kynurenine-formamidase.

PTM databases

iPTMnetiQ04066.

Proteomic databases

MaxQBiQ04066.

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.
OrthoDBiEOG7NSBCS.

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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast."
    Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S., Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.
    Mol. Cell. Proteomics 3:209-225(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A SERINE HYDROLASE, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  5. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence."
    Wogulis M., Chew E.R., Donohoue P.D., Wilson D.K.
    Biochemistry 47:1608-1621(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution."
    Arndt J.W., Schwarzenbacher R., Page R., Abdubek P., Ambing E., Biorac T., Canaves J.M., Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., Hale J., Hampton E., Han G.W.
    , Haugen J., Hornsby M., Klock H.E., Koesema E., Kreusch A., Kuhn P., Jaroszewski L., Lesley S.A., Levin I., McMullan D., McPhillips T.M., Miller M.D., Morse A., Moy K., Nigoghossian E., Ouyang J., Peti W.S., Quijano K., Reyes R., Sims E., Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J., von Delft F., Wang X., West B., White A., Wolf G., Xu Q., Zagnitko O., Hodgson K.O., Wooley J., Wilson I.A.
    Proteins 58:755-758(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

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: June 8, 2016
This is version 118 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.