ID H3BDW9_LATCH Unreviewed; 269 AA.
AC H3BDW9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:ENSLACP00000020090.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000020090.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000020090.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 -!- 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 ---------------------------------------------------------------------------
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; AFYH01017047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BDW9; -.
DR ESTHER; latch-h3bdx0; Kynurenine-formamidase.
DR Ensembl; ENSLACT00000020228.1; ENSLACP00000020090.1; ENSLACG00000017657.2.
DR GeneTree; ENSGT00390000011093; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000017657; Expressed in chordate pharynx and 6 other cell types or 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; 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 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:UP000008672};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_03014}.
FT DOMAIN 41..141
FT /note="BD-FAE-like"
FT /evidence="ECO:0000259|Pfam:PF20434"
FT MOTIF 60..64
FT /note="HGGXW"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 129
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 212
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 244
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
SQ SEQUENCE 269 AA; 29753 MW; ACC19D2603277D9A CRC64;
MDKDAVIEAH VKWVTEGTKV ARSITQVMLG VPYGAGDGDK LDVYLPSHPP AALPLLVYLH
GGYWQFFSKE ESGFMAPPLV KKGIAVVAVD HDIAPKGNMD SIVSQVRRSV AFVVQQYSHI
SGIYLCGHSA GAHLVAMALA TDWKEYGVTP DIKGAFLVSG IYDLLPIVRT SVNDPLKMND
EIAVRNSPMQ LIPEVKRACE SCEIVIALGE HDSPEFRRQS REYYQALQSA GLKVHFEDIL
NTDHFNVIEQ LSDEGYRLTQ MILKMILEG
//
