ID KYNB_BACHK Reviewed; 209 AA. AC Q6HHX8; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 94. 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=BT9727_2522; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). 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=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_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; AE017355; AAT61841.1; -; Genomic_DNA. DR RefSeq; WP_000858066.1; NC_005957.1. DR RefSeq; YP_036848.1; NC_005957.1. DR AlphaFoldDB; Q6HHX8; -. DR SMR; Q6HHX8; -. DR KEGG; btk:BT9727_2522; -. DR PATRIC; fig|281309.8.peg.2670; -. DR HOGENOM; CLU_030671_3_1_9; -. DR UniPathway; UPA00333; UER00454. DR Proteomes; UP000001301; 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:0043420; P:anthranilate metabolic process; ISS:UniProtKB. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; ISS:UniProtKB. 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; Tryptophan catabolism; Zinc. FT CHAIN 1..209 FT /note="Kynurenine formamidase" FT /id="PRO_0000362093" 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; 23104 MW; 757CC1F2F68A0975 CRC64; MKTSEWIDIS QPLNNDIATW PGDTPFSYEV SWSKEESGSV NVGKLTMSIH TGTHIDAPFH FDNNGKKVLD LDIQVYVGPT RIIDVSNLES IGKKELEKFH LEGVERLLLR TSSHGKANEF PDIIPHLRAD IAPFLSEKGI RLIGVDVPSV DPLDDKELAA HHQLFKHGIH ILENVVLDHV ADGDYELIAL PLALSDADGS PVRAVIKPI //