ID E3D7H6_GARV3 Unreviewed; 484 AA.
AC E3D7H6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 Name=folC {ECO:0000313|EMBL:ADP39268.1};
GN OrderedLocusNames=HMPREF0421_21186 {ECO:0000313|EMBL:ADP39268.1};
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP39268.1, ECO:0000313|Proteomes:UP000001453};
RN [1] {ECO:0000313|EMBL:ADP39268.1, ECO:0000313|Proteomes:UP000001453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
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}.
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DR EMBL; CP002104; ADP39268.1; -; Genomic_DNA.
DR RefSeq; WP_013399731.1; NC_014644.1.
DR RefSeq; YP_003986291.1; NC_014644.1.
DR AlphaFoldDB; E3D7H6; -.
DR KEGG; gvg:HMPREF0421_21186; -.
DR PATRIC; fig|525284.18.peg.1167; -.
DR HOGENOM; CLU_015869_1_2_11; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000001453; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 56..293
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 317..388
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 484 AA; 53260 MW; EE43AE3A4EB0C898 CRC64;
MSMEHPNSNG ERIIDVERDI MRRAPEHNKT NLDLDRMRLI LDILGHPEQS MHVIHITGTN
GKGSTARMAE AICRAYGLRT GLYTSPHLQR VNERIMIDGE EISDDHFVDV YDQMKDIIDM
VDARMDADGK PRMSFFEVLT AMAIWAFADA PVDVAVMEVG MGGEWDATNV MNADAAIIGP
VDMDHMQWLG NTVEEIARTK AGIIKPNCTV ILGPQPHESQ VLPIIQEVAN RNNAKLLRDF
SDGSGELEVI SRTPAVGGQV ATLRTPNGTY EDVPIDKFGV HQAHNALAAL AAAEVVLPVN
GALDGDLVAE ALSQVKVPGR IEQVRTSPTI IIDGGHNVNA AESLRKTIEE NYNFEQLIGV
VAMMADKQVE EYLGVLEPIL TKIIVTRNSW RDRVMDPEDL EKIAVNVFGR DRVIRVDDLP
DAIQEAVNLV DEDDELGVGY GHGVLICGSF VTAGDARTML IERVNPDLKK PKDQRANTHP
NIAN
//
