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Database: UniProt
Entry: C2NIK8_BACCE
LinkDB: C2NIK8_BACCE
Original site: C2NIK8_BACCE 
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
//
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