ID M3YP96_MUSPF Unreviewed; 307 AA.
AC M3YP96;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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 Name=AFMID {ECO:0000256|HAMAP-Rule:MF_03014,
GN ECO:0000313|Ensembl:ENSMPUP00000013153.1,
GN ECO:0000313|RefSeq:XP_012909827.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000013153.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000013153.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_012909827.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_012909827.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|HAMAP-
CC Rule:MF_03014}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03014}.
CC Note=Predominantly cytosolic. Some fraction is nuclear.
CC {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}.
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DR EMBL; AEYP01025192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012909827.1; XM_013054373.2.
DR STRING; 9669.ENSMPUP00000013153; -.
DR ESTHER; muspf-m3yp96; Kynurenine-formamidase.
DR Ensembl; ENSMPUT00000013364.1; ENSMPUP00000013153.1; ENSMPUG00000013251.1.
DR GeneID; 101694456; -.
DR KEGG; mpuf:101694456; -.
DR CTD; 125061; -.
DR eggNOG; KOG4627; Eukaryota.
DR GeneTree; ENSGT00390000011093; -.
DR HOGENOM; CLU_012494_4_7_1; -.
DR OMA; HFDIVEN; -.
DR OrthoDB; 2880059at2759; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR013094; AB_hydrolase_3.
DR InterPro; IPR027519; KFase_ver/fungi-typ.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; KYNURENINE FORMAMIDASE; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03014};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03014};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03014};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_03014}.
FT DOMAIN 92..281
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT MOTIF 95..99
FT /note="HGGXW"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 249
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 281
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
SQ SEQUENCE 307 AA; 34217 MW; 591D123FD7A420F4 CRC64;
MEVPGRATGA EAPWKQLSAE ELENQYCPSR WVIRRGAEET LKMYTHLGDK ATKKVRATRK
SLLHVPYGDG EGEKLDIYFP GEVAAEGLPF CLFLHGGYWQ SGSKDMSAFM VEPLTARGVA
VVVVAYDIAP KGTLDQMIDQ VTRSIAFVQR KYPCNEGLYL CGHSAGAHLA AMMLLANWTK
HGVTPNLKGF FLVSGIYDLE PIVHTTQNAP LLLTPEDARR NSPQLLLEAA LARPSGPACR
VLVTVGQHDS PEFHRQSREF FQTLCRGGWD ASFEEIPDVD HFEIIWSLTQ QDFVLTQMIL
STILREL
//