ID A0A0M9VJK5_9FLAO Unreviewed; 404 AA.
AC A0A0M9VJK5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=AM493_17055 {ECO:0000313|EMBL:KOS07559.1};
OS Flavobacterium akiainvivens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS07559.1, ECO:0000313|Proteomes:UP000037755};
RN [1] {ECO:0000313|EMBL:KOS07559.1, ECO:0000313|Proteomes:UP000037755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IK-1 {ECO:0000313|EMBL:KOS07559.1,
RC ECO:0000313|Proteomes:UP000037755};
RA Wan X., Hou S., Saito J., Donachie S.;
RT "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL Submitted (AUG-2015) 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:KOS07559.1}.
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DR EMBL; LIYD01000005; KOS07559.1; -; Genomic_DNA.
DR RefSeq; WP_054409266.1; NZ_LIYD01000005.1.
DR AlphaFoldDB; A0A0M9VJK5; -.
DR STRING; 1202724.AM493_17055; -.
DR PATRIC; fig|1202724.3.peg.3542; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000037755; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037755}.
FT DOMAIN 51..192
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 404 AA; 44050 MW; 3735E01152932D84 CRC64;
MTYKETTEWM FGRLPMYQMQ GAVAYKADLA NTLLLAAHLG NPENKLKTIH VAGTNGKGSV
SSMLASILQE AGYKVGLYTS PHLKDFRERI KINGEDISEA FIVDFVAKNK AFFEANDLSF
FEMTVGLAFD YFVQENIDIA VVETGMGGRL DSTNIITPLV SVITNIGMDH TQFLGNTLQA
IAGEKAGIIK PGTPVVVGEY TPETKPVFES KASEKRSAIY FAQDEVLPDY PSALLGDYQR
QNKKTVLKTV EVLQSALSIN GDAVKTGLLN VIKNTGLRGR WEQIHTNPAA IADTAHNSHG
LKPVMAQLLN QKYTSLHIVF GVVNDKNLDE VLPLLPKKAT YYFAKPGVPR GLDAQILANA
AKKYNLNGKI FESVKQAYDA ALQQAAPDGL VYVGGSTFVV AEIL
//
