ID G3H3F6_CRIGR Unreviewed; 335 AA.
AC G3H3F6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=I79_004773 {ECO:0000313|EMBL:EGV97891.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV97891.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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; JH000126; EGV97891.1; -; Genomic_DNA.
DR AlphaFoldDB; G3H3F6; -.
DR STRING; 10029.G3H3F6; -.
DR ESTHER; crigr-g3h3f6; Kynurenine-formamidase.
DR PaxDb; 10029-XP_007634147-1; -.
DR eggNOG; KOG4627; Eukaryota.
DR InParanoid; G3H3F6; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000001075; Unassembled WGS sequence.
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:UP000001075};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_03014}.
FT DOMAIN 74..262
FT /note="BD-FAE-like"
FT /evidence="ECO:0000259|Pfam:PF20434"
FT MOTIF 93..97
FT /note="HGGXW"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 162
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 247
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 279
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
SQ SEQUENCE 335 AA; 36979 MW; 59DF926E42B40710 CRC64;
MAASALPAGE PPWKTLSAEE LERQYSPSRW VIRMKAEEVV STFVRTGSQA TRKARATRRN
QLDVPYGDGE GEKMDIYFPD EHSQASPLLL FFHGGYWQSG SKDDSAFMVN PLTAQGVGVA
IVAYDIAPKG TLDQMVDQVT RSVVFLQRRY PSNGGIYLCG HSAGAHLAAM VLLAGWTKHG
VTPNLQGFLL VSGIYDLEPL IYTSQNAPLH MTLEDAQRNS PQHCLEVAPA KPVGPACPVL
VVVGQHDSPE FHRQSREFYE MLHRVGWKAS FQELPGVDHF DIIENLTQED DVLTQTILKT
IFPDALRTPG LQPVCTSENL QKMRLPPNTG LSVCP
//
