KFA_SALSA
ID KFA_SALSA Reviewed; 294 AA.
AC B5XB27;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
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=afmid;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC Rule:MF_03014}. Nucleus {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; BT048246; ACI68047.1; -; mRNA.
DR RefSeq; NP_001134570.1; NM_001141098.3.
DR RefSeq; XP_014038735.1; XM_014183260.1.
DR AlphaFoldDB; B5XB27; -.
DR SMR; B5XB27; -.
DR STRING; 8030.ENSSSAP00000002061; -.
DR ESTHER; salsa-afmid; Kynurenine-formamidase.
DR GeneID; 100196069; -.
DR KEGG; sasa:100196069; -.
DR CTD; 125061; -.
DR OMA; WSHRMAA; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000087266; Chromosome ssa02.
DR Bgee; ENSSSAG00000001106; Expressed in liver and 15 other tissues.
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; -; 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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..294
FT /note="Kynurenine formamidase"
FT /id="PRO_0000361879"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..88
FT /note="HGGXW"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 236
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 269
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
SQ SEQUENCE 294 AA; 32682 MW; 8ABC38B02E85DF67 CRC64;
MSRWKDMNKD ELERQFSPSQ WSHRMSADDV IKSHVTALKE GTERARGLAQ TLLNVPYGEG
EGEKLDVYVP TTTSLDVPLV IYLHGGYWQF LSKEESGFMA VPLVHKGVVV VAVGYDIAPK
GNMDVMVSQV RRSVVSVIQQ YSHISGLYLC GHSAGAHLAA MILSTDWSQY SVTPQIKGAF
LVSGIYDLLP ILSTYVNEPL KMTEEVALRN SPSQLVPQLK LSSSNCDIVV AVAQNDSPEF
RKQSEDYYKA LESTEGLKVT LEDVPNTDHF NIIEQLVDGD YHLTQLLLKM MGKS
