ID L1PMU8_9FLAO Unreviewed; 389 AA.
AC L1PMU8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HMPREF9073_01808 {ECO:0000313|EMBL:EKY16750.1};
OS Capnocytophaga sp. oral taxon 326 str. F0382.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1035193 {ECO:0000313|EMBL:EKY16750.1, ECO:0000313|Proteomes:UP000010441};
RN [1] {ECO:0000313|EMBL:EKY16750.1, ECO:0000313|Proteomes:UP000010441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0382 {ECO:0000313|EMBL:EKY16750.1,
RC ECO:0000313|Proteomes:UP000010441};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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 -!- 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:EKY16750.1}.
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DR EMBL; AMEU01000120; EKY16750.1; -; Genomic_DNA.
DR AlphaFoldDB; L1PMU8; -.
DR STRING; 1035193.HMPREF9073_01808; -.
DR PATRIC; fig|1035193.3.peg.1687; -.
DR eggNOG; COG0285; Bacteria.
DR HOGENOM; CLU_015869_1_1_10; -.
DR Proteomes; UP000010441; 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; 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; PF08245; Mur_ligase_M; 1.
DR PIRSF; PIRSF001563; Folylpolyglu_synth; 2.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 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 36..213
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 389 AA; 42837 MW; 213A51772CB09E43 CRC64;
MFQTQGKTAL NNKLDNILAF TSVLGNPQTK FKSLHIAGTN GKGSSSSMLA SILQEAGYKV
GLYTSPHLKD FRERIKINGK EIPEDYVVSF IAKNKPFLEE YHLSFFEMTV GMAFSYFENE
KVDIAVIEVG LGGRFDSTNI ITPEVSLITN ISKDHTDILG DTLPKIAFEK AGIIKRNVPV
VISEYQEETA PVFTAKAKEM NAPIIFANHI ETSLTTDLQG AYQEKNIKGV IAVTELLIHQ
GWDITPENIA QGLLHVVHNT NLKGRWQTLG SYPTIVCDTG HNVGGLTYVM EQLKKQTYTH
LHIVVGFVKE KDVNSVLELF PEEATYYFCS PAIARGLNVD TLKEIATAKG LQGKRYSSVV
EALNAAKAQA LPTDFIFVGG STFVVAEVL
//
