ID G3A5B9_9RALS Unreviewed; 205 AA.
AC G3A5B9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 13-SEP-2023, entry version 44.
DE RecName: Full=Kynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_01969};
DE Short=KFA {ECO:0000256|HAMAP-Rule:MF_01969};
DE Short=KFase {ECO:0000256|HAMAP-Rule:MF_01969};
DE EC=3.5.1.9 {ECO:0000256|HAMAP-Rule:MF_01969};
DE AltName: Full=Arylformamidase {ECO:0000256|HAMAP-Rule:MF_01969};
DE AltName: Full=N-formylkynurenine formamidase {ECO:0000256|HAMAP-Rule:MF_01969};
DE Short=FKF {ECO:0000256|HAMAP-Rule:MF_01969};
GN Name=kynB {ECO:0000256|HAMAP-Rule:MF_01969};
GN ORFNames=RALSY_30917 {ECO:0000313|EMBL:CCA89149.1};
OS Ralstonia syzygii R24.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA89149.1};
RN [1] {ECO:0000313|EMBL:CCA89149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA89149.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA89149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA89149.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002204, ECO:0000256|HAMAP-
CC Rule:MF_01969}.
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:0000256|ARBA:ARBA00000640, ECO:0000256|HAMAP-
CC Rule:MF_01969};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01969};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01969}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01969}.
CC -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. KynB family.
CC {ECO:0000256|HAMAP-Rule:MF_01969}.
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DR EMBL; FR854088; CCA89149.1; -; Genomic_DNA.
DR AlphaFoldDB; G3A5B9; -.
DR UniPathway; UPA00333; UER00454.
DR GO; GO:0004061; F:arylformamidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004328; F:formamidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.30.50; Putative cyclase; 1.
DR HAMAP; MF_01969; KynB; 1.
DR InterPro; IPR007325; KFase/CYL.
DR InterPro; IPR037175; KFase_sf.
DR InterPro; IPR017484; Kynurenine_formamidase_bac.
DR NCBIfam; TIGR03035; trp_arylform; 1.
DR PANTHER; PTHR31118; CYCLASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR31118:SF32; KYNURENINE FORMAMIDASE; 1.
DR Pfam; PF04199; Cyclase; 1.
DR SUPFAM; SSF102198; Putative cyclase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01969};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01969};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_01969};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01969}.
FT ACT_SITE 55
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01969"
SQ SEQUENCE 205 AA; 22005 MW; D580A99E2FD674A9 CRC64;
MWDISPTLST ATPTWPGDTP FSQEIAWKLE GDCPVNVGRI TLSPHTGAHA DAPLHYRADG
APIGAVPLDA YLGPCRVIHC VGVARVEPEH VRDALDGTPP RVLLRTYARM PQSAWDDRFA
AIAPETIELL AAHGVRLIGT DTASLDPQTS KTMDAHHAVG RHGLAILEGL VLDDVPAGDY
ELIALPLKFA TLDASPVRAV LRRLP
//