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Database: UniProt
Entry: A0A0D2G0M2_9EURO
LinkDB: A0A0D2G0M2_9EURO
Original site: A0A0D2G0M2_9EURO 
ID   A0A0D2G0M2_9EURO        Unreviewed;       339 AA.
AC   A0A0D2G0M2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Kynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_03014};
DE            Short=KFA {ECO:0000256|HAMAP-Rule:MF_03014};
DE            Short=KFase {ECO:0000256|HAMAP-Rule:MF_03014};
DE            EC=3.5.1.9 {ECO:0000256|HAMAP-Rule:MF_03014};
DE   AltName: Full=Arylformamidase {ECO:0000256|HAMAP-Rule:MF_03014};
DE   AltName: Full=N-formylkynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_03014};
DE            Short=FKF {ECO:0000256|HAMAP-Rule:MF_03014};
GN   ORFNames=PV04_07907 {ECO:0000313|EMBL:KIW65669.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW65669.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW65669.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW65669.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03014}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03014}.
CC   -!- SIMILARITY: Belongs to the kynurenine formamidase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03014}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03014}.
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DR   EMBL; KN846960; KIW65669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2G0M2; -.
DR   ESTHER; 9euro-a0a0d2fcd8; Kynurenine-formamidase.
DR   HOGENOM; CLU_016852_0_0_1; -.
DR   OrthoDB; 1423424at2759; -.
DR   UniPathway; UPA00333; UER00454.
DR   Proteomes; UP000054266; 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; alpha/beta hydrolase; 1.
DR   HAMAP; MF_03014; KFase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR049492; BD-FAE-like_dom.
DR   InterPro; IPR027519; KFase_ver/fungi-typ.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF34; KYNURENINE FORMAMIDASE; 1.
DR   Pfam; PF20434; BD-FAE; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03014};
KW   Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW   Rule:MF_03014}.
FT   DOMAIN          144..278
FT                   /note="BD-FAE-like"
FT                   /evidence="ECO:0000259|Pfam:PF20434"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT   ACT_SITE        313
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
SQ   SEQUENCE   339 AA;  37679 MW;  4904F599BB0439A3 CRC64;
     MGTSPPQTSG QRDMSRPQTP DKVLRGITRH QYAQDNILQS YELYIPELDH KHQADAKGHK
     YWVIFIHGGY FRDPSVTSSS FYPALGILAP ESNHHHIFKN NGHGSRLSDI TPYISAYASL
     NYRLSPHPGK APQDPHTTPA YELRNAEWPE HIHDVLAAIA HLQSKYGFGE RYLLVGHSVG
     ATMGLLSALA AQKAPFSTTC HLDMPTIEPP MAILGVSGIY DFPLIHESVP DYVELTRNAI
     HNEADFALAS PAKYTAKDYV DIWTAGGEKK RALVIAHSRD DGWVDWKQVE AMENALKSQS
     AVDVRVSEMK GQHNEIWEKG TELARVVVEA VGVMRGLEA
//
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