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Kynurenine formamidase (KFA) (KFase) (EC 3.5.1.9) (Arylformamidase) (Biosynthesis of nicotinic acid protein 7) (N-formylkynurenine formamidase) (FKF)

 KFA_YEAST               Reviewed;         261 AA.
Q04066; D6VT57;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 129.
RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_03014};
Short=KFA {ECO:0000255|HAMAP-Rule:MF_03014};
Short=KFase {ECO:0000255|HAMAP-Rule:MF_03014};
EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_03014};
AltName: Full=Arylformamidase {ECO:0000255|HAMAP-Rule:MF_03014};
AltName: Full=Biosynthesis of nicotinic acid protein 7;
AltName: Full=N-formylkynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_03014};
Short=FKF {ECO:0000255|HAMAP-Rule:MF_03014};
Name=BNA7 {ECO:0000255|HAMAP-Rule:MF_03014};
OrderedLocusNames=YDR428C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
IDENTIFICATION AS A SERINE HYDROLASE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=14645503; DOI=10.1074/mcp.M300082-MCP200;
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.;
"Synergistic computational and experimental proteomics approaches for
more accurate detection of active serine hydrolases in yeast.";
Mol. Cell. Proteomics 3:209-225(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[6]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
PubMed=18205391; DOI=10.1021/bi701172v;
Wogulis M., Chew E.R., Donohoue P.D., Wilson D.K.;
"Identification of formyl kynurenine formamidase and kynurenine
aminotransferase from Saccharomyces cerevisiae using crystallographic,
bioinformatic and biochemical evidence.";
Biochemistry 47:1608-1621(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[9]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
PubMed=15624212; DOI=10.1002/prot.20336;
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.;
"Crystal structure of an alpha/beta serine hydrolase (YDR428C) from
Saccharomyces cerevisiae at 1.85 A resolution.";
Proteins 58:755-758(2005).
-!- FUNCTION: 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. {ECO:0000255|HAMAP-Rule:MF_03014,
ECO:0000269|PubMed:18205391}.
-!- CATALYTIC ACTIVITY: N-formyl-L-kynurenine + H(2)O = formate + L-
kynurenine. {ECO:0000255|HAMAP-Rule:MF_03014,
ECO:0000269|PubMed:18205391}.
-!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
{ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:18205391}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03014}.
-!- DOMAIN: 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. {ECO:0000269|PubMed:18205391}.
-!- DISRUPTION PHENOTYPE: Cells exhibit slow growth in the absence of
nicotinate. {ECO:0000269|PubMed:18205391}.
-!- SIMILARITY: Belongs to the kynurenine formamidase family.
{ECO:0000255|HAMAP-Rule:MF_03014}.
-----------------------------------------------------------------------
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EMBL; U33007; AAB64885.1; -; Genomic_DNA.
EMBL; BK006938; DAA12267.1; -; Genomic_DNA.
PIR; S69709; S69709.
RefSeq; NP_010716.3; NM_001180736.3.
PDB; 1VKH; X-ray; 1.85 A; A/B=1-261.
PDBsum; 1VKH; -.
ProteinModelPortal; Q04066; -.
SMR; Q04066; -.
BioGrid; 32486; 29.
DIP; DIP-4139N; -.
IntAct; Q04066; 1.
STRING; 4932.YDR428C; -.
ESTHER; yeast-YDR428C; Kynurenine-formamidase.
iPTMnet; Q04066; -.
MaxQB; Q04066; -.
PaxDb; Q04066; -.
PRIDE; Q04066; -.
EnsemblFungi; YDR428C; YDR428C; YDR428C.
GeneID; 852038; -.
KEGG; sce:YDR428C; -.
EuPathDB; FungiDB:YDR428C; -.
SGD; S000002836; BNA7.
HOGENOM; HOG000065929; -.
InParanoid; Q04066; -.
KO; K14263; -.
OMA; HSCSAHM; -.
OrthoDB; EOG092C48GX; -.
BioCyc; YEAST:MONOMER3O-17; -.
BRENDA; 3.5.1.9; 984.
UniPathway; UPA00333; UER00454.
EvolutionaryTrace; Q04066; -.
PRO; PR:Q04066; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0004061; F:arylformamidase activity; IDA:SGD.
GO; GO:0009056; P:catabolic process; IBA:GO_Central.
GO; GO:0009435; P:NAD biosynthetic process; IDA:SGD.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.1820; -; 1.
HAMAP; MF_03014; KFase; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013094; AB_hydrolase_3.
InterPro; IPR027519; KFase_ver/fungi-typ.
Pfam; PF07859; Abhydrolase_3; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Phosphoprotein;
Reference proteome; Tryptophan catabolism.
CHAIN 1 261 Kynurenine formamidase.
/FTId=PRO_0000234660.
MOTIF 36 40 HGGXW.
ACT_SITE 110 110 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_03014}.
ACT_SITE 211 211 {ECO:0000255|HAMAP-Rule:MF_03014}.
ACT_SITE 243 243 {ECO:0000255|HAMAP-Rule:MF_03014}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
HELIX 15 17 {ECO:0000244|PDB:1VKH}.
STRAND 19 22 {ECO:0000244|PDB:1VKH}.
STRAND 30 35 {ECO:0000244|PDB:1VKH}.
TURN 39 41 {ECO:0000244|PDB:1VKH}.
HELIX 47 50 {ECO:0000244|PDB:1VKH}.
HELIX 51 60 {ECO:0000244|PDB:1VKH}.
STRAND 66 71 {ECO:0000244|PDB:1VKH}.
TURN 76 78 {ECO:0000244|PDB:1VKH}.
HELIX 83 99 {ECO:0000244|PDB:1VKH}.
STRAND 104 109 {ECO:0000244|PDB:1VKH}.
HELIX 111 120 {ECO:0000244|PDB:1VKH}.
HELIX 121 124 {ECO:0000244|PDB:1VKH}.
TURN 127 129 {ECO:0000244|PDB:1VKH}.
HELIX 132 141 {ECO:0000244|PDB:1VKH}.
STRAND 144 151 {ECO:0000244|PDB:1VKH}.
HELIX 156 162 {ECO:0000244|PDB:1VKH}.
HELIX 164 166 {ECO:0000244|PDB:1VKH}.
HELIX 167 173 {ECO:0000244|PDB:1VKH}.
HELIX 178 180 {ECO:0000244|PDB:1VKH}.
HELIX 185 199 {ECO:0000244|PDB:1VKH}.
STRAND 202 208 {ECO:0000244|PDB:1VKH}.
HELIX 217 228 {ECO:0000244|PDB:1VKH}.
STRAND 233 238 {ECO:0000244|PDB:1VKH}.
HELIX 243 248 {ECO:0000244|PDB:1VKH}.
HELIX 250 258 {ECO:0000244|PDB:1VKH}.
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


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