KYNB_BURCC
ID KYNB_BURCC Reviewed; 213 AA.
AC B1JXI7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969};
DE Short=KFA {ECO:0000255|HAMAP-Rule:MF_01969};
DE Short=KFase {ECO:0000255|HAMAP-Rule:MF_01969};
DE EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_01969};
DE AltName: Full=Arylformamidase {ECO:0000255|HAMAP-Rule:MF_01969};
DE AltName: Full=N-formylkynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969};
DE Short=FKF {ECO:0000255|HAMAP-Rule:MF_01969};
GN Name=kynB {ECO:0000255|HAMAP-Rule:MF_01969};
GN OrderedLocusNames=Bcenmc03_2601;
OS Burkholderia cenocepacia (strain MC0-3).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=406425;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC0-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL Submitted (FEB-2008) 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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_01969};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01969};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01969}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01969}.
CC -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family.
CC {ECO:0000255|HAMAP-Rule:MF_01969}.
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DR EMBL; CP000958; ACA91762.1; -; Genomic_DNA.
DR RefSeq; WP_012329112.1; NC_010508.1.
DR AlphaFoldDB; B1JXI7; -.
DR SMR; B1JXI7; -.
DR EnsemblBacteria; ACA91762; ACA91762; Bcenmc03_2601.
DR KEGG; bcm:Bcenmc03_2601; -.
DR HOGENOM; CLU_030671_3_1_4; -.
DR OMA; GHPTHKT; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000002169; Chromosome 1.
DR GO; GO:0004061; F:arylformamidase activity; ISS:UniProtKB.
DR GO; GO:0004328; F:formamidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043420; P:anthranilate metabolic process; ISS:UniProtKB.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; ISS:UniProtKB.
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 PANTHER; PTHR31118; PTHR31118; 1.
DR Pfam; PF04199; Cyclase; 1.
DR SUPFAM; SSF102198; SSF102198; 1.
DR TIGRFAMs; TIGR03035; trp_arylform; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Tryptophan catabolism; Zinc.
FT CHAIN 1..213
FT /note="Kynurenine formamidase"
FT /id="PRO_0000362101"
FT ACT_SITE 58
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
SQ SEQUENCE 213 AA; 22662 MW; EDFC1F20167A178B CRC64;
MDTLWDISPP VSPATPVWPG DTPVAVERVW RMEAGSPVNV ARLTLSPHTG AHCDAPLHYD
ADGAPIGAVP LDTYLGPCRV IHCIGASPVV RPADVEVALD GVPPRVLLRT YARAAVEQWD
SAFCAVAPDT VDLLAAHGVK LIGIDTPSLD PQESKTMDAH HRVRAHRMAI LEGIVLDDVP
PGDYELIALP LKFATLDASP VRAVLRALPA HAS
