ID C2NIK8_BACCE Unreviewed; 209 AA.
AC C2NIK8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
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 ORFNames=bcere0004_25310 {ECO:0000313|EMBL:EEK56078.1};
OS Bacillus cereus BGSC 6E1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK56078.1};
RN [1] {ECO:0000313|EMBL:EEK56078.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK56078.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(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. {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 -!- 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:EEK56078.1}.
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DR EMBL; ACLU01000065; EEK56078.1; -; Genomic_DNA.
DR RefSeq; WP_000858063.1; NZ_CM000716.1.
DR AlphaFoldDB; C2NIK8; -.
DR SMR; C2NIK8; -.
DR HOGENOM; CLU_030671_3_1_9; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000000284; 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 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 {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 60
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
SQ SEQUENCE 209 AA; 23103 MW; CA036F6C827DA597 CRC64;
MKTSEWIDIS QPLNNDIATW PGDTPFSYEV SWSKEESGSV NVGKLTMSIH TGTHIDAPFH
FDNEGKKVID LDVQVYVGPA RIIDVSNLES IGKKELEKFH LEGVERLLLR TSSHGKANEF
PDIIPHLRAD IAPFLSEKGI RLIGVDVPSV DPLDDKELAA HHQLFKHGIH ILENVVLDHV
ADGDYELIAL PLALSDADGS PVRAVIRPI
//