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Database: UniProt
Entry: A0A0R1V0V1_9LACO
LinkDB: A0A0R1V0V1_9LACO
Original site: A0A0R1V0V1_9LACO 
ID   A0A0R1V0V1_9LACO        Unreviewed;       437 AA.
AC   A0A0R1V0V1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=FD50_GL000406 {ECO:0000313|EMBL:KRL99126.1};
OS   Liquorilactobacillus satsumensis DSM 16230 = JCM 12392.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423801 {ECO:0000313|EMBL:KRL99126.1, ECO:0000313|Proteomes:UP000051166};
RN   [1] {ECO:0000313|EMBL:KRL99126.1, ECO:0000313|Proteomes:UP000051166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16230 {ECO:0000313|EMBL:KRL99126.1,
RC   ECO:0000313|Proteomes:UP000051166};
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:KRL99126.1}.
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DR   EMBL; AZFQ01000034; KRL99126.1; -; Genomic_DNA.
DR   RefSeq; WP_056960590.1; NZ_AZFQ01000034.1.
DR   AlphaFoldDB; A0A0R1V0V1; -.
DR   STRING; 1423801.FD50_GL000406; -.
DR   PATRIC; fig|1423801.4.peg.413; -.
DR   OrthoDB; 9809356at2; -.
DR   Proteomes; UP000051166; 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          42..264
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          294..364
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   437 AA;  48235 MW;  99766D7656E2F309 CRC64;
     MANDTTKKLP SFLYGQGDRI ALLKRVLHQL GHPDEKFKII HVCGTNGKGS TSTMIAALLQ
     KMGERTGLFT SPFIDEVTES IRIDDTMISA ASFAGYVKVI TAVLVKMELD PAALSAFEMT
     FVVAMLYFAE HRVAYVVLEC GLGGELDATN AVKTTAYSIF TKIGLDHTRI LGTTIAEIAV
     TKSKIIRAHA EVIIAPKQPP QVYTILAQQA RRMAAQVHLA ATVELRVVAT AQTKTFMQLK
     TAHAECTFEY SLLGTYQQEN LATVLRWLQV FLAKEKRNFK LEQLIAKTMP SLSIPGRFEK
     IKTAPLIILD AAHNLDGIKA FTATVNTLYP EKPKKIVVGF LKDKDYGHCV AKLLEIKNAS
     FYLTEPEHPT RKLAAVELQQ VFDKISRMHA PAFTAARQAF NQAVAAAKEE DGLILVVGSF
     YLLKAVRKLI VPKNKEG
//
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