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Database: UniProt
Entry: A0A0R2LLH5_9LACO
LinkDB: A0A0R2LLH5_9LACO
Original site: A0A0R2LLH5_9LACO 
ID   A0A0R2LLH5_9LACO        Unreviewed;       195 AA.
AC   A0A0R2LLH5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   ORFNames=IV66_GL000037 {ECO:0000313|EMBL:KRO02613.1};
OS   Ligilactobacillus pobuzihii.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=449659 {ECO:0000313|EMBL:KRO02613.1, ECO:0000313|Proteomes:UP000051886};
RN   [1] {ECO:0000313|EMBL:KRO02613.1, ECO:0000313|Proteomes:UP000051886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103219 {ECO:0000313|EMBL:KRO02613.1,
RC   ECO:0000313|Proteomes:UP000051886};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRO02613.1}.
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DR   EMBL; JQCN01000001; KRO02613.1; -; Genomic_DNA.
DR   RefSeq; WP_017868018.1; NZ_JQCN01000001.1.
DR   AlphaFoldDB; A0A0R2LLH5; -.
DR   STRING; 449659.IV66_GL000037; -.
DR   PATRIC; fig|449659.4.peg.37; -.
DR   OrthoDB; 9801938at2; -.
DR   Proteomes; UP000051886; Unassembled WGS sequence.
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   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361279};
KW   Ligase {ECO:0000313|EMBL:KRO02613.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361279};
KW   Metal-binding {ECO:0000256|RuleBase:RU361279};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361279};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051886}.
SQ   SEQUENCE   195 AA;  21668 MW;  E402FF7CFCEFF8A1 CRC64;
     MFSKEFMRKQ QLDKLKLQAK CWSKLGGELA IYQELLSSEI WKNATTVGMT LSEPYEFDTK
     PLITAALNSG KIVAVPRTLP HRQLQFCRLL PKIEAGRSNF GVLEPVIGTP QISLNELDLL
     VVPGLAFSAA GARLGFGGGF YDRILGKYKG EVVSCAESAR FFSETKWETE ITDQEIPNIL
     TVSGWFSKNG GEFKK
//
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