KYNB_BURCJ
ID KYNB_BURCJ Reviewed; 213 AA.
AC B4E9I9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=BceJ2315_27280; ORFNames=BCAL2790;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ZINC IONS, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVE SITE,
RP 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=0.57 mM for N-formyl-L-kynurenine {ECO:0000269|PubMed:24942958};
CC Vmax=58.15 nmol/min/mg enzyme {ECO:0000269|PubMed:24942958};
CC Note=kcat is 43.94 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}.
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DR EMBL; AM747720; CAR53090.1; -; Genomic_DNA.
DR RefSeq; WP_012492838.1; NC_011000.1.
DR PDB; 4COG; X-ray; 1.60 A; A/B/C/D=1-213.
DR PDBsum; 4COG; -.
DR AlphaFoldDB; B4E9I9; -.
DR SMR; B4E9I9; -.
DR STRING; 216591.BCAL2790; -.
DR EnsemblBacteria; CAR53090; CAR53090; BCAL2790.
DR GeneID; 56559163; -.
DR KEGG; bcj:BCAL2790; -.
DR eggNOG; COG1878; Bacteria.
DR HOGENOM; CLU_030671_3_1_4; -.
DR OMA; GHPTHKT; -.
DR OrthoDB; 831439at2; -.
DR BioCyc; BCEN216591:G1G1V-3091-MON; -.
DR BRENDA; 3.5.1.9; 8982.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000001035; Chromosome 1.
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; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Tryptophan catabolism; Zinc.
FT CHAIN 1..213
FT /note="Kynurenine formamidase"
FT /id="PRO_0000362103"
FT ACT_SITE 58
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969,
FT ECO:0000305|PubMed:24942958"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4COG"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4COG"
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:4COG"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4COG"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4COG"
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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4COG"
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,
FT ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4COG"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:4COG"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:4COG"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4COG"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4COG"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:4COG"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:4COG"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4COG"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4COG"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:4COG"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:4COG"
SQ SEQUENCE 213 AA; 22671 MW; 569C8F1FEEE7BD05 CRC64;
MDTLWDISPP VSPATPVWPG DTPVAVERVW RMEAGSPVNV ARLTLSPHTG AHCDAPLHYD
ADGAPIGAVP LDTYLGPCRV IHCIGAAPVV RPADVEAALD GVPPRVLLRT YARAAVEQWD
SNFCAVAPDT VDLLAAHGVK LIGIDTPSLD PQESKTMDAH RRVRAHRMAI LEGIVLDDVP
PGDYELIALP LKFATLDASP VRAVLRALPA QAS
