KYNB_PSEAE
ID KYNB_PSEAE Reviewed; 213 AA.
AC Q9I234;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
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, 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, ECO:0000303|PubMed:14592712};
GN OrderedLocusNames=PA2081;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) IN COMPLEX WITH ZINC IONS, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, COFACTOR,
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:14592712, 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:14592712, 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=0.98 mM for N-formyl-L-kynurenine {ECO:0000269|PubMed:24942958};
CC Vmax=147.99 nmol/min/mg enzyme {ECO:0000269|PubMed:24942958};
CC Note=kcat is 114.21 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, ECO:0000305|PubMed:14592712}.
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; AE004091; AAG05469.1; -; Genomic_DNA.
DR PIR; E83386; E83386.
DR RefSeq; NP_250771.1; NC_002516.2.
DR RefSeq; WP_003114853.1; NZ_QZGE01000022.1.
DR PDB; 4COB; X-ray; 2.37 A; A/B=1-213.
DR PDBsum; 4COB; -.
DR AlphaFoldDB; Q9I234; -.
DR SMR; Q9I234; -.
DR STRING; 287.DR97_5766; -.
DR PaxDb; Q9I234; -.
DR PRIDE; Q9I234; -.
DR DNASU; 878591; -.
DR EnsemblBacteria; AAG05469; AAG05469; PA2081.
DR GeneID; 878591; -.
DR KEGG; pae:PA2081; -.
DR PATRIC; fig|208964.12.peg.2173; -.
DR PseudoCAP; PA2081; -.
DR HOGENOM; CLU_030671_3_1_6; -.
DR InParanoid; Q9I234; -.
DR OMA; GHPTHKT; -.
DR PhylomeDB; Q9I234; -.
DR BioCyc; PAER208964:G1FZ6-2119-MON; -.
DR BRENDA; 3.5.1.9; 5087.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000002438; 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; IMP:PseudoCAP.
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..213
FT /note="Kynurenine formamidase"
FT /id="PRO_0000362130"
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: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 ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4COB"
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:4COB"
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:4COB"
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:4COB"
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:4COB"
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:4COB"
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:4COB"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4COB"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4COB"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4COB"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4COB"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4COB"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4COB"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4COB"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4COB"
SQ SEQUENCE 213 AA; 23152 MW; 49C2EC78FF055773 CRC64;
MTSLRYWDIS PALDPNTPTW PGDTPFQQEW AARLDEQCPV NVGRITLSPH TGAHVDGPLH
YRADGLPIGQ VPLDIYMGPC RVIHCIGANP LVTPEHLAGQ LDDLPSRVLL RTFERVPANW
PEGFCAIAPA TIECLAERGV RLVGIDTPSL DPQHSKTLDA HHAVGRHGMA ILEGVVLDDV
PAGDYELLAL PLKFTHLDAS PVRAVLRALP TAE
