KFA_YEAST
ID KFA_YEAST Reviewed; 261 AA.
AC Q04066; D6VT57;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_03014};
DE Short=KFA {ECO:0000255|HAMAP-Rule:MF_03014};
DE Short=KFase {ECO:0000255|HAMAP-Rule:MF_03014};
DE EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_03014};
DE AltName: Full=Arylformamidase {ECO:0000255|HAMAP-Rule:MF_03014};
DE AltName: Full=Biosynthesis of nicotinic acid protein 7;
DE AltName: Full=N-formylkynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_03014};
DE Short=FKF {ECO:0000255|HAMAP-Rule:MF_03014};
GN Name=BNA7 {ECO:0000255|HAMAP-Rule:MF_03014}; OrderedLocusNames=YDR428C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION AS A SERINE HYDROLASE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT "Synergistic computational and experimental proteomics approaches for more
RT accurate detection of active serine hydrolases in yeast.";
RL Mol. Cell. Proteomics 3:209-225(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=18205391; DOI=10.1021/bi701172v;
RA Wogulis M., Chew E.R., Donohoue P.D., Wilson D.K.;
RT "Identification of formyl kynurenine formamidase and kynurenine
RT aminotransferase from Saccharomyces cerevisiae using crystallographic,
RT bioinformatic and biochemical evidence.";
RL Biochemistry 47:1608-1621(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=15624212; DOI=10.1002/prot.20336;
RA Arndt J.W., Schwarzenbacher R., Page R., Abdubek P., Ambing E., Biorac T.,
RA Canaves J.M., Chiu H.-J., Dai X., Deacon A.M., DiDonato M., Elsliger M.-A.,
RA Godzik A., Grittini C., Grzechnik S.K., Hale J., Hampton E., Han G.W.,
RA Haugen J., Hornsby M., Klock H.E., Koesema E., Kreusch A., Kuhn P.,
RA Jaroszewski L., Lesley S.A., Levin I., McMullan D., McPhillips T.M.,
RA Miller M.D., Morse A., Moy K., Nigoghossian E., Ouyang J., Peti W.S.,
RA Quijano K., Reyes R., Sims E., Spraggon G., Stevens R.C., van den Bedem H.,
RA Velasquez J., Vincent J., von Delft F., Wang X., West B., White A.,
RA Wolf G., Xu Q., Zagnitko O., Hodgson K.O., Wooley J., Wilson I.A.;
RT "Crystal structure of an alpha/beta serine hydrolase (YDR428C) from
RT Saccharomyces cerevisiae at 1.85 A resolution.";
RL Proteins 58:755-758(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-
CC kynurenine, the second step in the kynurenine pathway of tryptophan
CC degradation. Kynurenine may be further oxidized to nicotinic acid,
CC NAD(H) and NADP(H). Required for elimination of toxic metabolites.
CC {ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:18205391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine;
CC Xref=Rhea:RHEA:13009, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57959, ChEBI:CHEBI:58629; EC=3.5.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03014,
CC ECO:0000269|PubMed:18205391};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:18205391}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03014}.
CC -!- DOMAIN: The main chain amide nitrogen atoms of the second glycine and
CC its adjacent residue in the HGGXW motif define the oxyanion hole, and
CC stabilize the oxyanion that forms during the nucleophilic attack by the
CC catalytic serine during substrate cleavage.
CC {ECO:0000269|PubMed:18205391}.
CC -!- DISRUPTION PHENOTYPE: Cells exhibit slow growth in the absence of
CC nicotinate. {ECO:0000269|PubMed:18205391}.
CC -!- SIMILARITY: Belongs to the kynurenine formamidase family.
CC {ECO:0000255|HAMAP-Rule:MF_03014}.
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DR EMBL; U33007; AAB64885.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12267.1; -; Genomic_DNA.
DR PIR; S69709; S69709.
DR RefSeq; NP_010716.3; NM_001180736.3.
DR PDB; 1VKH; X-ray; 1.85 A; A/B=1-261.
DR PDBsum; 1VKH; -.
DR AlphaFoldDB; Q04066; -.
DR SMR; Q04066; -.
DR BioGRID; 32486; 32.
DR DIP; DIP-4139N; -.
DR IntAct; Q04066; 1.
DR STRING; 4932.YDR428C; -.
DR ESTHER; yeast-YDR428C; Kynurenine-formamidase.
DR iPTMnet; Q04066; -.
DR MaxQB; Q04066; -.
DR PaxDb; Q04066; -.
DR PRIDE; Q04066; -.
DR EnsemblFungi; YDR428C_mRNA; YDR428C; YDR428C.
DR GeneID; 852038; -.
DR KEGG; sce:YDR428C; -.
DR SGD; S000002836; BNA7.
DR VEuPathDB; FungiDB:YDR428C; -.
DR eggNOG; ENOG502S28Q; Eukaryota.
DR HOGENOM; CLU_016852_1_0_1; -.
DR InParanoid; Q04066; -.
DR OMA; NARWPDH; -.
DR BioCyc; YEAST:MON3O-17; -.
DR BRENDA; 3.5.1.9; 984.
DR UniPathway; UPA00333; UER00454.
DR EvolutionaryTrace; Q04066; -.
DR PRO; PR:Q04066; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04066; protein.
DR GO; GO:0004061; F:arylformamidase activity; IDA:SGD.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:SGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_03014; KFase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR027519; KFase_ver/fungi-typ.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Phosphoprotein; Reference proteome;
KW Tryptophan catabolism.
FT CHAIN 1..261
FT /note="Kynurenine formamidase"
FT /id="PRO_0000234660"
FT MOTIF 36..40
FT /note="HGGXW"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 211
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1VKH"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1VKH"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1VKH"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1VKH"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1VKH"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:1VKH"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1VKH"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:1VKH"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:1VKH"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:1VKH"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:1VKH"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:1VKH"
SQ SEQUENCE 261 AA; 29991 MW; F07FE52DD9D2EF92 CRC64;
MSNTVRAISP DITLFNKTLT FQEISQNTRE AVIYIHGGAW NDPENTPNDF NQLANTIKSM
DTESTVCQYS IEYRLSPEIT NPRNLYDAVS NITRLVKEKG LTNINMVGHS VGATFIWQIL
AALKDPQEKM SEAQLQMLGL LQIVKRVFLL DGIYSLKELL VEYPEYDCFT RLAFPDGIQM
YEEEPSRVMP YVKKALSRFS IDMHLVHSYS DELLTLRQTN CLISCLQDYQ LSFKLYLDDL
GLHNDVYKNG KVAKYIFDNI C
