ID B9J2Y8_BACCQ Unreviewed; 209 AA.
AC B9J2Y8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 OrderedLocusNames=BCQ_2599 {ECO:0000313|EMBL:ACM13027.1};
OS Bacillus cereus (strain Q1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM13027.1, ECO:0000313|Proteomes:UP000000441};
RN [1] {ECO:0000313|EMBL:ACM13027.1, ECO:0000313|Proteomes:UP000000441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:ACM13027.1,
RC ECO:0000313|Proteomes:UP000000441};
RX PubMed=19060151; DOI=10.1128/JB.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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}.
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DR EMBL; CP000227; ACM13027.1; -; Genomic_DNA.
DR AlphaFoldDB; B9J2Y8; -.
DR KEGG; bcq:BCQ_2599; -.
DR HOGENOM; CLU_030671_3_1_9; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000000441; 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; 23133 MW; 25D11B059BEA0978 CRC64;
MKTSEWIDIS QPLNNDIATW PGDTPFSYEV SWSKEESGSV NVGKLTMSIH TGTHIDAPFH
FDNDGKKVLD LDIQVYVGPT RIIDVSNLES IGKKELEKFH LEGVERLLLR TSSHGKANEF
PDIIPHLRAD IAPFLSEKGI RLIGVDVPSV DPLDDKELAA HHQLFKHGIH ILENVVLDHV
ADGDYELIAL PLALSDADGS PVRAVIRPI
//
