KYNB_ERYLH
ID KYNB_ERYLH Reviewed; 216 AA.
AC Q2N5X0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=ELI_14145;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(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: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; CP000157; ABC64921.1; -; Genomic_DNA.
DR RefSeq; WP_011415743.1; NC_007722.1.
DR AlphaFoldDB; Q2N5X0; -.
DR SMR; Q2N5X0; -.
DR STRING; 314225.ELI_14145; -.
DR EnsemblBacteria; ABC64921; ABC64921; ELI_14145.
DR KEGG; eli:ELI_14145; -.
DR eggNOG; COG1878; Bacteria.
DR HOGENOM; CLU_030671_3_1_5; -.
DR OMA; GHPTHKT; -.
DR OrthoDB; 831439at2; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000008808; Chromosome.
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; Reference proteome; Tryptophan catabolism; Zinc.
FT CHAIN 1..216
FT /note="Kynurenine formamidase"
FT /id="PRO_0000362123"
FT ACT_SITE 64
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 24
FT /ligand="substrate"
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 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
SQ SEQUENCE 216 AA; 24015 MW; 2927D2E5E8149777 CRC64;
MSSWKSQRRI WDISQTLRPG LPIWPGDTEF GFERTWRMDE GSPVNVGRMT MSTHSGTHGD
APLHYAEDGL DAASMELDSY IGECLVVDAR GVSGEIDVAD LPHIESADRV LFRQWDSFPH
DEWRSDWLPI AAETVEWLAL QGVKLIGTDA PSVDPQESKT MSAHKAVLKH DMRILEGLVL
DDVPEGRYEL LALPLKIVDG DAGLCRAILR ELPDAG
