KFA_PICGU
ID KFA_PICGU Reviewed; 259 AA.
AC A5DNX8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 62.
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=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}; ORFNames=PGUG_04979;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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 -!- 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}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_03014}.
CC -!- SIMILARITY: Belongs to the kynurenine formamidase family.
CC {ECO:0000255|HAMAP-Rule:MF_03014}.
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DR EMBL; CH408160; EDK40881.2; -; Genomic_DNA.
DR RefSeq; XP_001483024.1; XM_001482974.1.
DR AlphaFoldDB; A5DNX8; -.
DR SMR; A5DNX8; -.
DR STRING; 4929.XP_001483024.1; -.
DR ESTHER; picgu-bna7; Kynurenine-formamidase.
DR EnsemblFungi; EDK40881; EDK40881; PGUG_04979.
DR GeneID; 5125016; -.
DR KEGG; pgu:PGUG_04979; -.
DR VEuPathDB; FungiDB:PGUG_04979; -.
DR eggNOG; ENOG502S28Q; Eukaryota.
DR HOGENOM; CLU_016852_1_0_1; -.
DR InParanoid; A5DNX8; -.
DR OMA; NARWPDH; -.
DR OrthoDB; 992858at2759; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0004061; F:arylformamidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Hydrolase; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..259
FT /note="Kynurenine formamidase"
FT /id="PRO_0000361883"
FT MOTIF 34..38
FT /note="HGGXW"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 196
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 228
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
SQ SEQUENCE 259 AA; 29091 MW; 949D4D76B64A8318 CRC64;
MSSSKLLKYG SDDLQTIRVY RHDSGNHLSI IFIHGGAWRD PRNTFNDFEE LVGKLPSTIN
TFGINYRLSP AVKHPAHLED VVSAIEYLAK NYKVENVGLV GHSVGATLAL QILNYKTILP
GLERPLGIKM KFLVFLDGIY DVPKLVEEYP TYSSFVNEAF KTKQDYMRAT PVSSEMPQFD
ISVEKCVILL VQSTEDELLS VQQTELMADF LQAKSIPFEK HLGAFGAHEQ VYRHHKVAKL
ITDAIGANLD GLVRARPQN
