ID A0A369HBY3_9HYPO Unreviewed; 283 AA.
AC A0A369HBY3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
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=CP533_2074 {ECO:0000313|EMBL:RDA95098.1};
OS Ophiocordyceps camponoti-saundersi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA95098.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA95098.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA95098.1,
RC ECO:0000313|Proteomes:UP000253071};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) 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 -!- 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:0000256|HAMAP-
CC Rule:MF_03014}.
CC -!- SIMILARITY: Belongs to the kynurenine formamidase family.
CC {ECO:0000256|HAMAP-Rule:MF_03014}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDA95098.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDHQ01000008; RDA95098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369HBY3; -.
DR STRING; 2039874.A0A369HBY3; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000253071; 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 Reference proteome {ECO:0000313|Proteomes:UP000253071};
KW Signal {ECO:0000256|SAM:SignalP};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_03014}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..283
FT /note="Kynurenine formamidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017059195"
FT DOMAIN 39..143
FT /note="BD-FAE-like"
FT /evidence="ECO:0000259|Pfam:PF20434"
FT MOTIF 50..54
FT /note="HGGXW"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 136
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 263
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
SQ SEQUENCE 283 AA; 31146 MW; DF5DA565D75FE884 CRC64;
MKPSLLLTLL SPLAEASFQL LSYGPHPRHV VGVWKDDKVD QASSWIIYIH GGAWRRQEDS
WRDFEPSVNN MLTSGLFPAT TFASIDYRLS PCAYPNANPC PFPVQHPDHI MDVRAALQML
AQQQGLRSNY LLIGHSAGAT LSFQLLMGEA ALEGQPLIDA PLPVAVIGIA GLYDLRGIND
RFGGAYSDFL TKAFGTDWRV WDRASPARFP GSFRQRLPPP GRVLLARSPQ DSLVDEPELD
NMARKLAADG VTLSVVKTLT GEHNSVWEDG NQIAGLVASV FRR
//
