ID   KFA_VANPO               Reviewed;         261 AA.
AC   A7TJ85;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Kpol_1004p28;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480400; EDO17654.1; -; Genomic_DNA.
DR   RefSeq; XP_001645512.1; XM_001645462.1.
DR   AlphaFoldDB; A7TJ85; -.
DR   SMR; A7TJ85; -.
DR   STRING; 436907.A7TJ85; -.
DR   ESTHER; vanpo-bna7; Kynurenine-formamidase.
DR   EnsemblFungi; EDO17654; EDO17654; Kpol_1004p28.
DR   GeneID; 5545893; -.
DR   KEGG; vpo:Kpol_1004p28; -.
DR   eggNOG; ENOG502S28Q; Eukaryota.
DR   HOGENOM; CLU_016852_1_0_1; -.
DR   InParanoid; A7TJ85; -.
DR   OMA; NARWPDH; -.
DR   OrthoDB; 992858at2759; -.
DR   PhylomeDB; A7TJ85; -.
DR   UniPathway; UPA00333; UER00454.
DR   Proteomes; UP000000267; 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..261
FT                   /note="Kynurenine formamidase"
FT                   /id="PRO_0000361885"
FT   MOTIF           33..37
FT                   /note="HGGXW"
FT   ACT_SITE        112
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
SQ   SEQUENCE   261 AA;  30049 MW;  222B0368A9D94B99 CRC64;
     MNDPTDTLYH QTAIHKLAEI GKNCKHLGII FIHGGAWVDP LNTSNDFKGI AGEISKVIEN
     NNTQGFNISM FGIEYRLSPS VKHPIHITDV ITNTYKLINE YKIDILYIVG HSVGATLGLQ
     LATDNRDYLI KYSSQLHLIR STIQGLFLLD GIYSLQELLK EYPTYDSFIS KAFTNYELEF
     QDPKEYLDKE QQFIKNLSFY IIHSFQDELL TLRQTDYLVE LLKAKEISFN LSISDYGRHN
     DVYINDRVAK LIIFNILSNI N