ID A0A0D6DV64_9LACT Unreviewed; 171 AA.
AC A0A0D6DV64;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN ORFNames=LACPI_0195 {ECO:0000313|EMBL:CEN27395.1};
OS Lactococcus piscium MKFS47.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN27395.1, ECO:0000313|Proteomes:UP000033166};
RN [1] {ECO:0000313|Proteomes:UP000033166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA Andreevskaya M.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = (6R)-5,10-
CC methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC Evidence={ECO:0000256|RuleBase:RU361279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU361279};
CC -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC family. {ECO:0000256|ARBA:ARBA00010638, ECO:0000256|RuleBase:RU361279}.
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DR EMBL; LN774769; CEN27395.1; -; Genomic_DNA.
DR RefSeq; WP_047916471.1; NZ_LN774769.1.
DR AlphaFoldDB; A0A0D6DV64; -.
DR STRING; 1364.LP2241_10169; -.
DR KEGG; lpk:LACPI_0195; -.
DR HOGENOM; CLU_066245_2_2_9; -.
DR Proteomes; UP000033166; Chromosome I.
DR GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR InterPro; IPR002698; FTHF_cligase.
DR InterPro; IPR024185; FTHF_cligase-like_sf.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR02727; MTHFS_bact; 1.
DR PANTHER; PTHR23407:SF1; 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR PANTHER; PTHR23407; ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR PIRSF; PIRSF006806; FTHF_cligase; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR006806-
KW 1}; Ligase {ECO:0000313|EMBL:CEN27395.1};
KW Magnesium {ECO:0000256|RuleBase:RU361279};
KW Metal-binding {ECO:0000256|RuleBase:RU361279};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006806-1}.
FT BINDING 4..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 124..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 171 AA; 19699 MW; 04E6CCFC80644942 CRC64;
MKKKAEIRKK MKFLLRNFNL AEKQAQTRKI FDQFFASDSY KTAKVIAVFL PMAFEFDMTS
ILTDKSKRIV IPKTLPNYQM IFTDYEPDKL VMTAFGVKES RDAISVTPDL IIVPGLAWSN
VGYRIGFGGG YYDRYLANFK GDTVSLVYDF QIVPDFQPEP FDIAISRLFK V
//
