KFA_PICST
ID KFA_PICST Reviewed; 268 AA.
AC A3GGU3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 25-MAY-2022, entry version 69.
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=PICST_66527;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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; AAVQ01000001; EAZ63982.2; -; Genomic_DNA.
DR RefSeq; XP_001388005.2; XM_001387968.1.
DR AlphaFoldDB; A3GGU3; -.
DR SMR; A3GGU3; -.
DR STRING; 4924.XP_001388005.2; -.
DR ESTHER; picst-bna7; Kynurenine-formamidase.
DR EnsemblFungi; EAZ63982; EAZ63982; PICST_66527.
DR GeneID; 4851492; -.
DR KEGG; pic:PICST_66527; -.
DR eggNOG; ENOG502S28Q; Eukaryota.
DR HOGENOM; CLU_016852_1_0_1; -.
DR InParanoid; A3GGU3; -.
DR OMA; NARWPDH; -.
DR OrthoDB; 992858at2759; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000002258; Chromosome 1.
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..268
FT /note="Kynurenine formamidase"
FT /id="PRO_0000361884"
FT MOTIF 33..37
FT /note="HGGXW"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 219
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 251
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
SQ SEQUENCE 268 AA; 31245 MW; C1E6053C938DD8ED CRC64;
MSEKIVFYGK EQLQRIRIFN YSESNDKTLI VLHGGGWRDP RNSYNDFEDM ANYILEEKKA
TNINIIGIDY RLSPFIKHPV HLIDVLTAFR YILENYKTGQ LSIVGHSVGA TLLLEILNYV
EIIQTGLEQL ETSEPSIEEL QTLFDFISKN LTFKTMYFLD GIYDVRALLE EYPSYDFFVK
SAFVSTVAIE EASQLSWKQH NEAFKIAVDK YEILHSLEDE LLSLNQPKLF AKYLQDRKIE
CSFRTGNWGE HEQVYRSQAV SEHVLQNM
