ID A0A0R1XPE0_9LACO Unreviewed; 433 AA.
AC A0A0R1XPE0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=FC91_GL001964 {ECO:0000313|EMBL:KRM28499.1};
OS Schleiferilactobacillus harbinensis DSM 16991.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM28499.1, ECO:0000313|Proteomes:UP000050949};
RN [1] {ECO:0000313|EMBL:KRM28499.1, ECO:0000313|Proteomes:UP000050949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM28499.1,
RC ECO:0000313|Proteomes:UP000050949};
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:KRM28499.1}.
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DR EMBL; AZFW01000032; KRM28499.1; -; Genomic_DNA.
DR RefSeq; WP_027827305.1; NZ_AZFW01000032.1.
DR AlphaFoldDB; A0A0R1XPE0; -.
DR PATRIC; fig|1122147.4.peg.2033; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000050949; 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; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050949}.
FT DOMAIN 44..274
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 299..357
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 433 AA; 47235 MW; 7BC7907100B6F413 CRC64;
MNYAEALTFI HSRPRLHRGH ELTWIKTFLA AIGHPEQQGR FIHITGTNGK GSVATMVTDM
LLAAGLHVGR FISPYITRFN ERIQVDGKDI SDTDLAAATT HLADVLAGMQ AANPDFALTE
FEFDTALGFY WFAQQQVDVA VIEVGIGGAH DKTNVIQPDV SAITTVGADH LELIGPTLAD
VAREKAGVIK PQTPVVLGDI AAEQTQIITT AAQAQAAPVA QLGRDFTVDH AHLHPADHAW
QFDYHRGDQD WTKLRLPSIS AYEVRNAAVA ITVAQLYLHG RGKTLDQATA QAGLMAFRWP
ARMELLHEQP YLMLDGAHNV PAAQALIKSI KAAFPGVTVH LIAAFLKDKD ATDMVRLYQR
AGWLITATEF PDARILPVTD WPETTVPINH VANWQEALAV ALQAASADDL ILFAGSLHFV
STVRNTLLKE DDP
//
