ID A0A0B0IL55_9BACI Unreviewed; 212 AA.
AC A0A0B0IL55;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=LQ50_02725 {ECO:0000313|EMBL:KHF41632.1};
OS Halalkalibacter okhensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF41632.1, ECO:0000313|Proteomes:UP000030832};
RN [1] {ECO:0000313|EMBL:KHF41632.1, ECO:0000313|Proteomes:UP000030832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA Prakash J.S.;
RT "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL Submitted (SEP-2014) 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 -!- 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:KHF41632.1}.
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DR EMBL; JRJU01000002; KHF41632.1; -; Genomic_DNA.
DR RefSeq; WP_034625762.1; NZ_JRJU01000002.1.
DR AlphaFoldDB; A0A0B0IL55; -.
DR STRING; 333138.LQ50_02725; -.
DR eggNOG; COG1878; Bacteria.
DR OrthoDB; 9796085at2; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000030832; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030832};
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 63
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 23
FT /ligand="substrate"
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 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
SQ SEQUENCE 212 AA; 23602 MW; 0F504A6E1CD39AD9 CRC64;
MRKQPNNAWI DVSQPLHDKL AHWPGDTPFS YQVTYSEEQT GSVNIGQMTM SVHSGTHVDA
PFHFRNDGAK ILDLDINVFI GEARVIELSS FEKIDKAALS TIDLDGVTRL LIKTAIPNRP
DRFPESIPYV TADGACYLHE KGIRLIGVDV PSVDALDSKE LEGHHALFQH QIHILENLML
DHVKEGDYEL IALPLPLKDA DGSPVRAVIR PL
//
