ID KYNB_BACCN Reviewed; 209 AA. AC A7GPY2; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 98. DE RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969}; DE Short=KFA {ECO:0000255|HAMAP-Rule:MF_01969}; DE Short=KFase {ECO:0000255|HAMAP-Rule:MF_01969}; DE EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_01969}; DE AltName: Full=Arylformamidase {ECO:0000255|HAMAP-Rule:MF_01969}; DE AltName: Full=N-formylkynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969}; DE Short=FKF {ECO:0000255|HAMAP-Rule:MF_01969}; GN Name=kynB {ECO:0000255|HAMAP-Rule:MF_01969}; GN OrderedLocusNames=Bcer98_1902; OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=315749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). 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. {ECO:0000255|HAMAP-Rule:MF_01969}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-formyl-L-kynurenine + H2O = L-kynurenine + formate + H(+); 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_01969}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01969}; CC Note=Binds 2 zinc ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01969}; 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_01969}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01969}. CC -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family. CC {ECO:0000255|HAMAP-Rule:MF_01969}. 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; CP000764; ABS22190.1; -; Genomic_DNA. DR RefSeq; WP_012094383.1; NC_009674.1. DR AlphaFoldDB; A7GPY2; -. DR SMR; A7GPY2; -. DR STRING; 315749.Bcer98_1902; -. DR PaxDb; 315749-Bcer98_1902; -. DR GeneID; 33897211; -. DR KEGG; bcy:Bcer98_1902; -. DR eggNOG; COG1878; Bacteria. DR HOGENOM; CLU_030671_3_1_9; -. DR OrthoDB; 9796085at2; -. DR UniPathway; UPA00333; UER00454. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0004061; F:arylformamidase activity; ISS:UniProtKB. DR GO; GO:0004328; F:formamidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006569; P:L-tryptophan catabolic process; ISS:UniProtKB. DR FunFam; 3.50.30.50:FF:000001; Kynurenine formamidase; 1. DR Gene3D; 3.50.30.50; Putative cyclase; 1. DR HAMAP; MF_01969; KynB; 1. DR InterPro; IPR007325; KFase/CYL. DR InterPro; IPR037175; KFase_sf. DR InterPro; IPR017484; Kynurenine_formamidase_bac. DR NCBIfam; TIGR03035; trp_arylform; 1. DR PANTHER; PTHR31118; CYCLASE-LIKE PROTEIN 2; 1. DR PANTHER; PTHR31118:SF32; KYNURENINE FORMAMIDASE; 1. DR Pfam; PF04199; Cyclase; 1. DR SUPFAM; SSF102198; Putative cyclase; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Reference proteome; Tryptophan catabolism; Zinc. FT CHAIN 1..209 FT /note="Kynurenine formamidase" FT /id="PRO_0000362090" FT ACT_SITE 60 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 20 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 54 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 161 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 173 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" FT BINDING 173 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969" SQ SEQUENCE 209 AA; 23004 MW; 502E2000368D7A1C CRC64; MKASEWIDIS QPLNNEIATW PGDTPFSYEV SCTKEQSGSV NIGKVTMSIH TGTHIDAPFH FDNDGKKVID LDIHVYVGPA RIIDVSSMDS IGVKELQQFN LEGVERLLLR TSSHGNAQKF PDIIPFLCAE IAPFLSKKGV RLIGVDVPSV DPLDDKELAA HHQLFQHGIH ILENVVLDHV QDGDYELIAL PLALTEADGS PVRAIIRPL //