ID E4V8K3_BIFBI Unreviewed; 546 AA.
AC E4V8K3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
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:EFR49945.1};
GN ORFNames=BBNG_00492 {ECO:0000313|EMBL:EFR49945.1};
OS Bifidobacterium bifidum NCIMB 41171.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=398513 {ECO:0000313|EMBL:EFR49945.1, ECO:0000313|Proteomes:UP000002776};
RN [1] {ECO:0000313|EMBL:EFR49945.1, ECO:0000313|Proteomes:UP000002776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 41171 {ECO:0000313|EMBL:EFR49945.1,
RC ECO:0000313|Proteomes:UP000002776};
RG The Broad Institute Genome Sequencing Platform;
RA Goulas T., Tzortzis G., Gibson G.R., Ward D., Mehta T., Young S., Jaffe D.,
RA Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA Birren B.;
RT "Annotation of Bifidobacterium bifidum strain NCIMB 41171.";
RL Submitted (AUG-2008) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS990229; EFR49945.1; -; Genomic_DNA.
DR RefSeq; WP_003812367.1; NZ_DS990229.1.
DR AlphaFoldDB; E4V8K3; -.
DR GeneID; 56627006; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_2_11; -.
DR Proteomes; UP000002776; 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}.
FT DOMAIN 146..289
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 313..385
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..546
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"
FT COMPBIAS 514..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 59152 MW; 47830A1A493337C0 CRC64;
MSFEHPNRNN ESIRDVERDI MRRPPEHNTT NLDLDRMNLM LDVLGHPEHS FRVIHVTGTN
GKGSTARMAE ALCRAYGLRT GLYTSPHLER INERIAIDGQ ELSDDDFVDM WDQIKDLVAI
VDAKMAESGR PPMSFFEVLT SMAIWKFADA PVDVAVVEVG MGGLWDATNV LDADAAIIGP
VDMDHMQWLG DTVEQIATEK AGIIKPNCTA IIGPQPHEER VMPILMEAAE RNHATLIRDG
YEMEVTDRVP AVGGQIATLH TPNGVYEQVP IAKFGEHQAH NALAALAAAE AVIPVNGPLN
GDLVGQALQG VKVPGRIEQI RTSPTIILDG GHNVNAAEAL RKAIEESYDF TQLVGVVAMM
GDKQVEEYLG VLEPILSQVV VTENSWRDRV MPAEELEKIA VQVFGRDRVI REDSLPDAIQ
KAVDMVDVED ETGVGYGRGV LVCGSFVTAG DARTLLKERM NADLAKPKAE RVNPSVGEPE
PRTGAGDPAR SGVESDADTD FATDANPDFN ENDFGDFGFD KAAKEAAKEA AKEADAADGG
PKGGQA
//
