ID A0A6F8TNB1_9BACI Unreviewed; 207 AA. AC A0A6F8TNB1; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 03-MAY-2023, entry version 8. DE RecName: Full=Kynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_01969}; DE Short=KFA {ECO:0000256|HAMAP-Rule:MF_01969}; DE Short=KFase {ECO:0000256|HAMAP-Rule:MF_01969}; DE EC=3.5.1.9 {ECO:0000256|HAMAP-Rule:MF_01969}; DE AltName: Full=Arylformamidase {ECO:0000256|HAMAP-Rule:MF_01969}; DE AltName: Full=N-formylkynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_01969}; DE Short=FKF {ECO:0000256|HAMAP-Rule:MF_01969}; GN Name=kynB {ECO:0000256|HAMAP-Rule:MF_01969, GN ECO:0000313|EMBL:BCB02356.1}; GN ORFNames=KH172YL63_04890 {ECO:0000313|EMBL:BCB02356.1}; OS Bacillus sp. KH172YL63. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=2709784 {ECO:0000313|EMBL:BCB02356.1, ECO:0000313|Proteomes:UP000500718}; RN [1] {ECO:0000313|EMBL:BCB02356.1, ECO:0000313|Proteomes:UP000500718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KH172YL63 {ECO:0000313|EMBL:BCB02356.1, RC ECO:0000313|Proteomes:UP000500718}; RA Murai Y., Masuda T., Onuma Y., Evans-Yamamoto D., Takeuchi N., Mori H., RA Masuyama N., Ishiguro S., Yachie D., Arakawa K.; RT "Complete Genome Sequence of Bacillus sp. Strain KH172YL63, Isolated from RT Deep-Sea Sediment."; RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00002204, ECO:0000256|HAMAP- CC 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:0000256|ARBA:ARBA00000640, ECO:0000256|HAMAP- CC Rule:MF_01969}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01969}; CC Note=Binds 2 zinc ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01969}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01969}. CC -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family. CC {ECO:0000256|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; AP022842; BCB02356.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6F8TNB1; -. DR UniPathway; UPA00333; UER00454. DR Proteomes; UP000500718; Chromosome. DR GO; GO:0004061; F:arylformamidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004328; F:formamidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway. 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 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. DR TIGRFAMs; TIGR03035; trp_arylform; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01969}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01969}; KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP- KW Rule:MF_01969}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01969}. FT ACT_SITE 57 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 17 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 158 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 170 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 170 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" SQ SEQUENCE 207 AA; 22661 MW; C98C4EDAB5DC6EE5 CRC64; MKIIDISRPL HNDTPVWPGD TPFSFSLNWT KEETGSVNVG QVTMSSHTGT HVDAPFHFDQ DGNRILDLPL ERFMGQAVVV SVEGAEEITP EQLKDIDFSG VTKILFKTNA WKNPDQFPEE IPPVSEELGP FLKQNGIDLI GVDLPSVDQL DSKELNAHHS LHANGIGILE GIVLTDVNPG RYELVALPLP LQDGDGSPVR AVLVERG //