KYNB_CUPMC
ID KYNB_CUPMC Reviewed; 218 AA.
AC P0C8P4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
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:14700627};
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=Rmet_2648;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND PATHWAY.
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=14700627; DOI=10.1016/j.chembiol.2003.11.011;
RA Kurnasov O., Goral V., Colabroy K., Gerdes S., Anantha S., Osterman A.,
RA Begley T.P.;
RT "NAD biosynthesis: identification of the tryptophan to quinolinate pathway
RT in bacteria.";
RL Chem. Biol. 10:1195-1204(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
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, ECO:0000269|PubMed:14700627}.
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:14700627};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01969,
CC ECO:0000305|PubMed:14700627};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01969};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA (PubMed:14700627,
CC PubMed:14592712). Insensitive to phenylmethylsulfonyl fluoride (PMSF)
CC (PubMed:14700627, PubMed:14592712). {ECO:0000269|PubMed:14592712,
CC ECO:0000269|PubMed:14700627}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for N-formyl-L-kynurenine {ECO:0000269|PubMed:14700627};
CC Note=kcat is 0.77 sec(-1) for N-formyl-L-kynurenine as substrate.
CC {ECO:0000269|PubMed:14700627};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:14700627};
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:0000269|PubMed:14592712,
CC ECO:0000305|PubMed:14700627}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CP000352; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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; CP000352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C8P4; -.
DR SMR; P0C8P4; -.
DR STRING; 266264.Rmet_6545; -.
DR eggNOG; COG1878; Bacteria.
DR SABIO-RK; P0C8P4; -.
DR UniPathway; UPA00333; UER00454.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0004061; F:arylformamidase activity; IDA:UniProtKB.
DR GO; GO:0004328; F:formamidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043420; P:anthranilate metabolic process; IDA:UniProtKB.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IDA: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 Hydrolase; Metal-binding; Reference proteome; Tryptophan catabolism; Zinc.
FT CHAIN 1..218
FT /note="Kynurenine formamidase"
FT /id="PRO_0000362135"
FT ACT_SITE 67
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01969"
SQ SEQUENCE 218 AA; 23383 MW; 43F8AEFAEA1959D9 CRC64;
MPQAPQLHDG RRIWDISPAV SPATPVWPGD TPFQHDPAWQ LDEHCPVNVG RITMSPHTGA
HADAPLHYAA DGAPIGAVPL DAYLGPCRVI HCIGAAPRVE PQHIAHALAG TPPRVLLRTY
AQAPQGKWDS AFCAVAPETI SLLARHGVRL IGIDTPSLDP ETSKTMDAHH AVRDHQLAIL
EGIVLDEVPA GDYELIALPL RLATLDASPV RAVLRELP
