KYNB_BACAN
ID KYNB_BACAN Reviewed; 209 AA.
AC Q81PP9; Q6HXW3; Q6KRY5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Kynurenine formamidase {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000303|PubMed:24942958};
DE Short=KFA {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000303|PubMed:24942958};
DE Short=KFase {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000303|PubMed:24942958};
DE EC=3.5.1.9 {ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000269|PubMed:24942958};
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=BA_2752, GBAA_2752, BAS2566;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, ACTIVE SITE, AND SUBUNIT.
RX PubMed=24942958; DOI=10.1042/bj20140511;
RA Diaz-Saez L., Srikannathasan V., Zoltner M., Hunter W.N.;
RT "Structures of bacterial kynurenine formamidase reveal a crowded binuclear
RT zinc catalytic site primed to generate a potent nucleophile.";
RL Biochem. J. 462:581-589(2014).
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:24942958}.
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:24942958};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01969,
CC ECO:0000269|PubMed:24942958};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01969,
CC ECO:0000269|PubMed:24942958};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for N-formyl-L-kynurenine {ECO:0000269|PubMed:24942958};
CC Vmax=65.41 nmol/min/mg enzyme {ECO:0000269|PubMed:24942958};
CC Note=kcat is 50.56 sec(-1) for N-formyl-L-kynurenine as substrate.
CC {ECO:0000269|PubMed:24942958};
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 ECO:0000269|PubMed:24942958}.
CC -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family.
CC {ECO:0000255|HAMAP-Rule:MF_01969}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016879; AAP26588.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT31868.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT54876.1; -; Genomic_DNA.
DR RefSeq; NP_845102.1; NC_003997.3.
DR RefSeq; WP_000858199.1; NZ_WXXJ01000026.1.
DR RefSeq; YP_028825.1; NC_005945.1.
DR PDB; 4CO9; X-ray; 1.95 A; A/B/C/D=1-209.
DR PDB; 4CZ1; X-ray; 2.24 A; A/B/C/D=1-209.
DR PDBsum; 4CO9; -.
DR PDBsum; 4CZ1; -.
DR AlphaFoldDB; Q81PP9; -.
DR SMR; Q81PP9; -.
DR STRING; 260799.BAS2566; -.
DR DNASU; 1087435; -.
DR EnsemblBacteria; AAP26588; AAP26588; BA_2752.
DR EnsemblBacteria; AAT31868; AAT31868; GBAA_2752.
DR GeneID; 45022594; -.
DR KEGG; ban:BA_2752; -.
DR KEGG; bar:GBAA_2752; -.
DR KEGG; bat:BAS2566; -.
DR PATRIC; fig|198094.11.peg.2736; -.
DR eggNOG; COG1878; Bacteria.
DR HOGENOM; CLU_030671_3_1_9; -.
DR OMA; MGKAVCF; -.
DR BRENDA; 3.5.1.9; 634.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; IDA:UniProtKB.
DR GO; GO:0043420; P:anthranilate metabolic process; IGC:UniProtKB.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IGC: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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome;
KW Tryptophan catabolism; Zinc.
FT CHAIN 1..209
FT /note="Kynurenine formamidase"
FT /id="PRO_0000362088"
FT ACT_SITE 60
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969,
FT ECO:0000305|PubMed:24942958"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24942958,
FT ECO:0007744|PDB:4CZ1"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9,
FT ECO:0007744|PDB:4CZ1"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9,
FT ECO:0007744|PDB:4CZ1"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9,
FT ECO:0007744|PDB:4CZ1"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9,
FT ECO:0007744|PDB:4CZ1"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9,
FT ECO:0007744|PDB:4CZ1"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9,
FT ECO:0007744|PDB:4CZ1"
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,
FT ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9,
FT ECO:0007744|PDB:4CZ1"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:4CO9"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 42..56
FT /evidence="ECO:0007829|PDB:4CO9"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4CO9"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4CO9"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4CO9"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4CO9"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4CO9"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4CO9"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4CO9"
SQ SEQUENCE 209 AA; 23188 MW; 7FDA0CE1FD44BA65 CRC64;
MKTSKWIDIS QPLNNDIATW PGDTPFSYEV LWSKEESGSV NVGKLTMSIH TGTHIDAPFH
FDNDGKKVLD LDIQVYVGPT RIIDVSNLES IGKKELEKFH LEGVERLLLR TSSHGKANEF
PDIIPHLRAD IAPFLSEKGI RLIGVDVPSV DPLDDKELAA HHQLFKHSIH ILENVVLDHV
ADGDYELIAL PLALSDADGS PVRAVIRPI
