ID A0A087DG74_9BIFI Unreviewed; 545 AA.
AC A0A087DG74;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=BSCA_1735 {ECO:0000313|EMBL:KFI94524.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI94524.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI94524.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI94524.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KFI94524.1}.
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DR EMBL; JGZO01000007; KFI94524.1; -; Genomic_DNA.
DR RefSeq; WP_033519646.1; NZ_JGZO01000007.1.
DR AlphaFoldDB; A0A087DG74; -.
DR STRING; 158787.BSCA_1735; -.
DR GeneID; 85166241; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000029033; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008841; F:dihydrofolate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:KFI94524.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029033}.
FT DOMAIN 146..289
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 313..384
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 58842 MW; 111C0DF1D0BE07C4 CRC64;
MSFEHPNRNN ETIRDVERDI MRRPPEHNTT NMDLDRMTLI LDLFGHPEES FRVIHITGTN
GKGSTARMAE AICRAYGMRT GLYTSPHLER INERIAIDGQ ELSDDDFVDS WDQIKDIVDL
VDARMEEQGK PRMSFFEVLT AMAIWKFADA PVDVAIVEVG MGGLQDATNV LNADAAVIGP
IDMDHMQWLG DTVQKIAEQK VGIIKPGCTA VIGRQPHEEE VMPIIEEAAR RNGATLVRDG
YEMEVGGRTP AVGGQIATLT TPMGRYEDVP IAKFGEHQAH NALAALAAAE AVIPVSGALD
GELVAEALGG VKVPGRIEQV RTSPTIIIDG GHNVNAAEAL RAAIEESYDF QQLVGVVAMM
GDKQVEEYLG VLEPILSHIV VTENSWRDRV MPAEDLEKIA VGVFGPDRVT RVDSLPDAIQ
AAVDMVDVDD ELGVGYGRGV LICGSFVTAG DARVLLKERM NPDLAKPKAD RVEPNLGGAA
APKADEDAAD RDFDSDANPD FLEDDFGDFG LSKLAQEAAQ EEAQGHGRHG DEADGGPAAG
AGTDR
//
