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Database: UniProt
Entry: A0A0R1M6S4_9LACO
LinkDB: A0A0R1M6S4_9LACO
Original site: A0A0R1M6S4_9LACO 
ID   A0A0R1M6S4_9LACO        Unreviewed;       436 AA.
AC   A0A0R1M6S4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=tetrahydrofolate synthase {ECO:0000256|ARBA:ARBA00013025};
DE            EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE   AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN   ORFNames=FD04_GL002232 {ECO:0000313|EMBL:KRK99415.1};
OS   Secundilactobacillus odoratitofui DSM 19909 = JCM 15043.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1423776 {ECO:0000313|EMBL:KRK99415.1, ECO:0000313|Proteomes:UP000051160};
RN   [1] {ECO:0000313|EMBL:KRK99415.1, ECO:0000313|Proteomes:UP000051160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19909 {ECO:0000313|EMBL:KRK99415.1,
RC   ECO:0000313|Proteomes:UP000051160};
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)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC         glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738,
CC         Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:141005,
CC         ChEBI:CHEBI:456216; EC=6.3.2.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00029332};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001563}.
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:KRK99415.1}.
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DR   EMBL; AZEE01000010; KRK99415.1; -; Genomic_DNA.
DR   RefSeq; WP_056946429.1; NZ_AZEE01000010.1.
DR   AlphaFoldDB; A0A0R1M6S4; -.
DR   STRING; 1423776.FD04_GL002232; -.
DR   PATRIC; fig|1423776.4.peg.2262; -.
DR   OrthoDB; 9809356at2; -.
DR   Proteomes; UP000051160; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   NCBIfam; TIGR01499; folC; 1.
DR   PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR   PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001563};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001563};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT   DOMAIN          46..272
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          298..373
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   436 AA;  48280 MW;  52F76B27C8C71E7F CRC64;
     MVANYEEALA FIHGRTQFKK SDHLNRMKTF LAQLHDPQQH LSAIHVAGTN GKGSTVAYLR
     DLLMGDGLTV GTFTSPFLIR FNERISIDGQ PIADDDLVAL VNRIQPVVVD LDATYPEGGP
     TEFEIITAMM FLYFKDRVDV AVIEVGIGGL LDSTNVFTPE VAVITTIGFD HMKLLGNTLA
     AIAAQKAGII KAGVPVVAGR LPAEAMAVVT QTATQLHAPL YRVGEEIQTQ VQATRGWQEQ
     FDFQFGAQRL RKLRLSMLGD YQVDNASCAL AAFLCYQRAH HLNVDEKSVK QSLAKTVWAG
     RFEPVSKDPL IVIDGAHNEP AVEELTQLLK QRFKGTEIYL LFAVLADKQH DQMLATLRQV
     PNIHLILTTF AGPGQRQVTD PQQLAAQYQN DDRVTVMPNW QVAIGQITQQ MSDSDLFLIT
     GSLYFISDVR QFFMAP
//
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