ID D4BS09_BIFBR Unreviewed; 533 AA.
AC D4BS09;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
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:EFE88222.1};
GN ORFNames=BIFBRE_04900 {ECO:0000313|EMBL:EFE88222.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE88222.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE88222.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE88222.1,
RC ECO:0000313|Proteomes:UP000003191};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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:EFE88222.1}.
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DR EMBL; ACCG02000016; EFE88222.1; -; Genomic_DNA.
DR RefSeq; WP_003830582.1; NZ_JDUD01000005.1.
DR AlphaFoldDB; D4BS09; -.
DR STRING; 1685.RY69_563; -.
DR KEGG; bbrd:BBBR_1243; -.
DR PATRIC; fig|518634.20.peg.1303; -.
DR HOGENOM; CLU_015869_1_2_11; -.
DR Proteomes; UP000003191; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003191}.
FT DOMAIN 56..289
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 313..386
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 477..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 57379 MW; 3F2B52862A3A0A54 CRC64;
MSFEHPNRNN ESMRDVELDI MSRPPEHNTT NLDLDRMNLM LDILGHPEQS FRVIHVTGTN
GKGSTARMAE AICRAYGMRT GLYTSPHLEK VNERIAIDGQ QLSDDDFIDV WDQIKDLVAL
VDAKMEEQGK PKMSFFEVLT AMAIWKFADA PVDVAVVEVG MGGLWDATNV LNADAAVIGP
VDMDHMQWLG DTVEQIAGEK AGIIKPNCTA IIGAQPHEEA VMPILEEAAE RNHAMLVRDG
YEMTVSDRMA AVGGQVATLT TPNGTYEGVP IAKFGEHQAH NALAALAAAE VVIPVNGPLD
GDLVAEALGS VKIPGRIEQI RTSPTIILDG GHNVNAAEAL RKAIEESYDF KQLVGVVAMM
RDKQVEEYLG VLEPILSSVV VTENSWRERV MPADELEKIA VEVFGRDRVI KEPNLPDAIQ
TAVNMVDAED ELGVGYGHGV LVCGSFVTAG DARTMLAEHA SPTMQQAMAI HQPAVDLDDA
TDGHGDQPGA DTLEDNVSPD DFDVFDVLGL GDAAKNNNAD GSSDQDSSAG SDA
//