ID   KYNB_MARMM              Reviewed;         209 AA.
AC   Q0APM5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   02-SEP-2026, entry version 88.
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=Mmar10_1470;
OS   Maricaulis maris (strain MCS10) (Caulobacter maris).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Maricaulales; Maricaulaceae; Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) 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=N-formyl-L-kynurenine + H2O = L-kynurenine + formate + H(+);
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000449; ABI65762.1; -; Genomic_DNA.
DR   RefSeq; WP_011643409.1; NC_008347.1.
DR   AlphaFoldDB; Q0APM5; -.
DR   SMR; Q0APM5; -.
DR   STRING; 394221.Mmar10_1470; -.
DR   KEGG; mmr:Mmar10_1470; -.
DR   eggNOG; COG1878; Bacteria.
DR   HOGENOM; CLU_030671_3_1_5; -.
DR   OrthoDB; 9777007at2; -.
DR   UniPathway; UPA00333; UER00454.
DR   Proteomes; UP000001964; 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:0006569; P:L-tryptophan catabolic process; ISS:UniProtKB.
DR   FunFam; 3.50.30.50:FF:000001; Kynurenine formamidase; 1.
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; Metal-binding; Reference proteome; Tryptophan catabolism; Zinc.
FT   CHAIN           1..209
FT                   /note="Kynurenine formamidase"
FT                   /id="PRO_0000362125"
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   209 AA;  22546 MW;  A6FC281C63DC8BCA CRC64;
     MAKMWDISQT LRPDLPVWPG DTAFACDEVW SIGPDCPVQV SRLTLSTHSG AHADAPSHYD
     QAGDDIASTP LELYVGPCRL VTASGNGPHV QPADLDWAAI DGATRVLVRT YAKFPADDWD
     PDFRALHADT IERLAATGCR LIGVDAASLD PQTSKTMDAH HAVQRHDMRI LEGLVFDGVP
     DGHYELIALP LKIAGADAAP LRAVLRELP
//