KFA_ASHGO
ID KFA_ASHGO Reviewed; 241 AA.
AC Q759T3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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}; OrderedLocusNames=ADR190W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52110.1; -; Genomic_DNA.
DR RefSeq; NP_984286.1; NM_209639.1.
DR AlphaFoldDB; Q759T3; -.
DR SMR; Q759T3; -.
DR STRING; 33169.AAS52110; -.
DR ESTHER; ashgo-bna7; Kynurenine-formamidase.
DR EnsemblFungi; AAS52110; AAS52110; AGOS_ADR190W.
DR GeneID; 4620448; -.
DR KEGG; ago:AGOS_ADR190W; -.
DR eggNOG; ENOG502S28Q; Eukaryota.
DR HOGENOM; CLU_016852_1_0_1; -.
DR InParanoid; Q759T3; -.
DR OMA; NARWPDH; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0004061; F:arylformamidase activity; IBA:GO_Central.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:EnsemblFungi.
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..241
FT /note="Kynurenine formamidase"
FT /id="PRO_0000361880"
FT MOTIF 23..27
FT /note="HGGXW"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 191
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 223
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
SQ SEQUENCE 241 AA; 27250 MW; C00B4309ECDD6728 CRC64;
MQRDYTATEV FQESGPDAIV YLHGGAWIDV RNSPRDFAEL AARVREDAPL ASQYAVTYRL
SPEVQHPVHV ADCVEHISQL IVEKGIRKLH LLGHSVGATL CWQILTALPG DRRYPEGPDF
AMKLALVRSS LAHVFLVDGI YSLRALLEEY PDYDYFVNKA FKSLKDFEDP SESAERISAG
PILHVIHSYK DELLTLKQTQ YLTAVLTAHQ IPYKLYVDDL GLHEDVYRNE KVAAYIVAQL
P
