ID   E7RH12_9BACL            Unreviewed;       206 AA.
AC   E7RH12;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Kynurenine formamidase {ECO:0000256|ARBA:ARBA00014889};
DE            EC=3.5.1.9 {ECO:0000256|ARBA:ARBA00012930};
GN   ORFNames=GPDM_08800 {ECO:0000313|EMBL:EGA89750.1};
OS   Planococcus donghaensis MPA1U2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=933115 {ECO:0000313|EMBL:EGA89750.1, ECO:0000313|Proteomes:UP000003052};
RN   [1] {ECO:0000313|EMBL:EGA89750.1, ECO:0000313|Proteomes:UP000003052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPA1U2 {ECO:0000313|EMBL:EGA89750.1,
RC   ECO:0000313|Proteomes:UP000003052};
RX   PubMed=21994932; DOI=10.1128/JB.05983-11;
RA   Pearson M.D., Noller H.F.;
RT   "The Draft Genome of Planococcus donghaensis MPA1U2 Reveals Nonsporulation
RT   Pathways Controlled by a Conserved Spo0A Regulon.";
RL   J. Bacteriol. 193:6106-6106(2011).
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}.
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};
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:EGA89750.1}.
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DR   EMBL; AEPB01000030; EGA89750.1; -; Genomic_DNA.
DR   RefSeq; WP_008430649.1; NZ_AEPB01000030.1.
DR   AlphaFoldDB; E7RH12; -.
DR   eggNOG; COG1878; Bacteria.
DR   OrthoDB; 9796085at2; -.
DR   Proteomes; UP000003052; Unassembled WGS sequence.
DR   GO; GO:0004061; F:arylformamidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004328; F:formamidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR   Gene3D; 3.50.30.50; Putative cyclase; 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   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   206 AA;  23094 MW;  61B1DB3CD4606385 CRC64;
     MTRKIIDISM ELNAMTPEWP GDTPFSYELS VTKEQSGSVN IGKLQTSTHI GTHIDAPFHY
     NEQGLKTHEL PLDVYLTQAQ VMDVSGLEKI NLSDLKPLEK NVEAVLLKTT SWQDRNKFPD
     KWPIFEESIA KWMADNGVKL LGVDVPSVDP ETSKDLPMHQ AMNQHQRFIL EGIVLDEVSE
     GVYHLVALPL KIRGGEGSPV RAILHT
//