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Database: UniProt
Entry: M3YP96_MUSPF
LinkDB: M3YP96_MUSPF
Original site: M3YP96_MUSPF 
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
//
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