KFA_DROME
ID KFA_DROME Reviewed; 300 AA.
AC Q9VMC9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=KFase; ORFNames=CG9542;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=83140; DOI=10.1007/bf00484718;
RA Moore G.P., Sullivan D.T.;
RT "Biochemical and genetic characterization of kynurenine formamidase from
RT Drosophila melanogaster.";
RL Biochem. Genet. 16:619-634(1978).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-300 IN COMPLEX WITH INHIBITOR,
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22690733; DOI=10.1042/bj20120416;
RA Han Q., Robinson H., Li J.;
RT "Biochemical identification and crystal structure of kynurenine formamidase
RT from Drosophila melanogaster.";
RL Biochem. J. 446:253-260(2012).
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:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:22690733,
CC ECO:0000269|PubMed:83140}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for N-formyl-L-kynurenine {ECO:0000269|PubMed:22690733};
CC Note=kcat is 1584 min(-1) with N-formyl-L-kynurenine as substrate.;
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 ECO:0000269|PubMed:22690733, ECO:0000269|PubMed:83140}.
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; AE014134; AAF52391.1; -; Genomic_DNA.
DR EMBL; AY089670; AAL90408.1; -; mRNA.
DR RefSeq; NP_001285676.1; NM_001298747.1.
DR RefSeq; NP_609036.1; NM_135192.2.
DR PDB; 4E11; X-ray; 2.00 A; A=1-300.
DR PDB; 4E14; X-ray; 1.64 A; A=1-300.
DR PDB; 4E15; X-ray; 1.50 A; A/B=1-300.
DR PDBsum; 4E11; -.
DR PDBsum; 4E14; -.
DR PDBsum; 4E15; -.
DR AlphaFoldDB; Q9VMC9; -.
DR SMR; Q9VMC9; -.
DR BioGRID; 60064; 5.
DR STRING; 7227.FBpp0078895; -.
DR ESTHER; drome-CG9542; Kynurenine-formamidase.
DR MEROPS; S09.A72; -.
DR PaxDb; Q9VMC9; -.
DR DNASU; 33907; -.
DR EnsemblMetazoa; FBtr0079265; FBpp0078895; FBgn0031821.
DR EnsemblMetazoa; FBtr0339785; FBpp0308832; FBgn0031821.
DR GeneID; 33907; -.
DR KEGG; dme:Dmel_CG9542; -.
DR UCSC; CG9542-RA; d. melanogaster.
DR CTD; 33907; -.
DR FlyBase; FBgn0287695; KFase.
DR VEuPathDB; VectorBase:FBgn0031821; -.
DR eggNOG; KOG4627; Eukaryota.
DR HOGENOM; CLU_012494_4_7_1; -.
DR InParanoid; Q9VMC9; -.
DR OMA; WSHRMAA; -.
DR OrthoDB; 992858at2759; -.
DR PhylomeDB; Q9VMC9; -.
DR BRENDA; 3.5.1.9; 1994.
DR UniPathway; UPA00333; UER00454.
DR BioGRID-ORCS; 33907; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33907; -.
DR PRO; PR:Q9VMC9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031821; Expressed in capitellum (Drosophila) and 16 other tissues.
DR ExpressionAtlas; Q9VMC9; baseline and differential.
DR Genevisible; Q9VMC9; DM.
DR GO; GO:0004061; F:arylformamidase activity; IDA:FlyBase.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..300
FT /note="Kynurenine formamidase"
FT /id="PRO_0000419492"
FT MOTIF 86..90
FT /note="HGGXW"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT ACT_SITE 276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03014"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4E14"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4E14"
FT HELIX 28..49
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4E15"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:4E15"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 125..145
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:4E15"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4E15"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4E15"
FT TURN 212..218
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 234..244
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:4E15"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4E15"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4E11"
FT HELIX 289..298
FT /evidence="ECO:0007829|PDB:4E15"
SQ SEQUENCE 300 AA; 34911 MW; 4631CC543FEEC935 CRC64;
MYNPRCKDLD RDYFPSYHTT RFQDQPEPNL AVLEHFVRVT KQHGRELTEK QGITVDHLRY
GEGRQLVDVF YSEKTTNQAP LFVFVHGGYW QEMDMSMSCS IVGPLVRRGY RVAVMDYNLC
PQVTLEQLMT QFTHFLNWIF DYTEMTKVSS LTFAGHSAGA HLLAQILMRP NVITAQRSKM
VWALIFLCGV YDLRELSNLE SVNPKNILGL NERNIESVSP MLWEYTDVTV WNSTKIYVVA
AEHDSTTFIE QSRHYADVLR KKGYKASFTL FKGYDHFDII EETAIDDSDV SRFLRNIEIE
