ID E9GB07_DAPPU Unreviewed; 298 AA.
AC E9GB07;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 ORFNames=DAPPUDRAFT_315847 {ECO:0000313|EMBL:EFX83454.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX83454.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX83454.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(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. 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 -!- 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; GL732537; EFX83454.1; -; Genomic_DNA.
DR AlphaFoldDB; E9GB07; -.
DR STRING; 6669.E9GB07; -.
DR ESTHER; dappu-e9gb07; Kynurenine-formamidase.
DR EnsemblMetazoa; EFX83454; EFX83454; DAPPUDRAFT_315847.
DR KEGG; dpx:DAPPUDRAFT_315847; -.
DR eggNOG; KOG4627; Eukaryota.
DR HOGENOM; CLU_012494_4_7_1; -.
DR InParanoid; E9GB07; -.
DR OMA; HFDIVEN; -.
DR PhylomeDB; E9GB07; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004061; F:arylformamidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03014};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_03014}.
FT DOMAIN 68..166
FT /note="BD-FAE-like"
FT /evidence="ECO:0000259|Pfam:PF20434"
FT MOTIF 86..90
FT /note="HGGXW"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 242
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
FT ACT_SITE 275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03014"
SQ SEQUENCE 298 AA; 33762 MW; 02E7B356E5125FF2 CRC64;
MEPEHWSFWD TQRLEDEYSP SKWSRRGPAD WVFDNHVKLV TQVSNQVKEE IQCDLDIPYG
KREGEKFDIF GAQLLPNDAP VFVYIHGGYW QALDRSISSY SVIPQFKAGH IVVVVGYELA
PKVGLKDIIL EIQSAISAVL KWAAERGSRS VVIAGHSAGS HLASMLLHDP QWQKSEPHLD
LLHGMVHISG VFDVIPLVAT SMNLPLNLDN ETAKLMSPLH CFNQSMEKVL NIKQLLVVGE
NDPTEFKRQT STYAQALLRA GFTDVHCKMM DSLDHFNIVE ELRNEDYELT RLIVKLIS
//
