KYNB_BACCR
ID KYNB_BACCR Reviewed; 209 AA.
AC Q81CK1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000303|PubMed:14592712};
DE Short=KFA {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000303|PubMed:14592712};
DE Short=KFase {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000303|PubMed:14592712};
DE EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000269|PubMed:14592712};
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, ECO:0000303|PubMed:14592712};
GN OrderedLocusNames=BC_2758;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=14592712; DOI=10.1016/s0378-1097(03)00684-0;
RA Kurnasov O., Jablonski L., Polanuyer B., Dorrestein P., Begley T.,
RA Osterman A.;
RT "Aerobic tryptophan degradation pathway in bacteria: novel kynurenine
RT formamidase.";
RL FEMS Microbiol. Lett. 227:219-227(2003).
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 ECO:0000269|PubMed:14592712}.
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 ECO:0000269|PubMed:14592712};
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, ECO:0000305|PubMed:14592712}.
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; AE016877; AAP09711.1; -; Genomic_DNA.
DR RefSeq; NP_832510.1; NC_004722.1.
DR RefSeq; WP_000858074.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81CK1; -.
DR SMR; Q81CK1; -.
DR STRING; 226900.BC_2758; -.
DR EnsemblBacteria; AAP09711; AAP09711; BC_2758.
DR GeneID; 67507396; -.
DR KEGG; bce:BC2758; -.
DR PATRIC; fig|226900.8.peg.2813; -.
DR HOGENOM; CLU_030671_3_1_9; -.
DR OMA; MGKAVCF; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0004061; F:arylformamidase activity; IDA: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; IGC:UniProtKB.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Tryptophan catabolism; Zinc.
FT CHAIN 1..209
FT /note="Kynurenine formamidase"
FT /id="PRO_0000362091"
FT ACT_SITE 60
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 50
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 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 173
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; 23066 MW; 54270A35415116A0 CRC64;
MKTSEWIDIS QPLNNNIATW PGDTPFSYEV SWSKEESGSV NVGKLTMSIH TGTHIDAPFH
FDNDGKKVLD LDVQVYVGPA RIIDVSNLES IGKKELESFH LEGVERLLLR TSSHGKAEEF
PEVIPHLRAD IASFLSEKGI RLIGVDVPSV DPLDDKELAA HHQLFKHGIH ILENVVLDHV
ADGDYELIAL PLALTDADGS PVRAVIRPI
