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Database: UniProt
Entry: D4BS09_BIFBR
LinkDB: D4BS09_BIFBR
Original site: D4BS09_BIFBR 
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
//
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