ID A0A2N2U8B0_9PROT Unreviewed; 208 AA. AC A0A2N2U8B0; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 11-DEC-2019, entry version 9. 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:PKO75929.1}; GN ORFNames=CVU21_15825 {ECO:0000313|EMBL:PKO75929.1}; OS Betaproteobacteria bacterium HGW-Betaproteobacteria-15. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=2013706 {ECO:0000313|EMBL:PKO75929.1, ECO:0000313|Proteomes:UP000233286}; RN [1] {ECO:0000313|EMBL:PKO75929.1, ECO:0000313|Proteomes:UP000233286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HGW-Betaproteobacteria-15 {ECO:0000313|EMBL:PKO75929.1}; RX PubMed=28350393; DOI=10.1038/ismej.2017.39; RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K., RA Probst A., Burstein D., Thomas B.C., Banfield J.F.; RT "Potential for microbial H2 and metal transformations associated with novel RT bacteria and archaea in deep terrestrial subsurface sediments."; RL ISME J. 11:1915-1929(2017). 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|HAMAP-Rule:MF_01969, CC ECO:0000256|SAAS:SAAS00902093}. 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_01969, CC ECO:0000256|SAAS:SAAS01115220}; 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, ECO:0000256|SAAS:SAAS00902092}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01969, CC ECO:0000256|SAAS:SAAS01062180}. CC -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family. CC {ECO:0000256|HAMAP-Rule:MF_01969, ECO:0000256|SAAS:SAAS01036644}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PKO75929.1}. 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; PHCR01000059; PKO75929.1; -; Genomic_DNA. DR UniPathway; UPA00333; UER00454. DR Proteomes; UP000233286; Unassembled WGS sequence. 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; -; 1. DR HAMAP; MF_01969; KynB; 1. DR InterPro; IPR007325; KFase/CYL. DR InterPro; IPR037175; KFase_sf. DR InterPro; IPR017484; Kynurenine_formamidase_bac. DR Pfam; PF04199; Cyclase; 1. DR SUPFAM; SSF102198; SSF102198; 1. DR TIGRFAMs; TIGR03035; trp_arylform; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01969, ECO:0000256|SAAS:SAAS00902098}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01969, KW ECO:0000256|SAAS:SAAS01062179}; KW Tryptophan catabolism {ECO:0000256|HAMAP-Rule:MF_01969, KW ECO:0000256|SAAS:SAAS00902095}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01969, ECO:0000256|SAAS:SAAS01062178}. FT ACT_SITE 58 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT METAL 48 FT /note="Zinc 1; via pros nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT METAL 52 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT METAL 54 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT METAL 54 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT METAL 160 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT METAL 172 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT METAL 172 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" FT BINDING 18 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969" SQ SEQUENCE 208 AA; 22353 MW; 870D5A7564690653 CRC64; MKKLWDISPP VNASTPIFPG DTAYAQQWVA SIEPGCPVNV SAITLSPHVG AHADAPLHYD PSGAAIGAVE LDAFLGPCRV IHAIGCGPLV RPEHLAHALD QLPPRVLVRV YEHMPQDRFD NALPAFAPET VALLADRGVL LIGIDSASID PADSKTLESH QVIRRRGLRV LENLLLDDVP EGDYELIALP LKLTTADASP VRAVLREL //