ID A0A085BPM0_9FLAO Unreviewed; 413 AA.
AC A0A085BPM0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=IO90_03740 {ECO:0000313|EMBL:KFC24415.1};
OS Chryseobacterium sp. FH1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1233951 {ECO:0000313|EMBL:KFC24415.1, ECO:0000313|Proteomes:UP000028641};
RN [1] {ECO:0000313|EMBL:KFC24415.1, ECO:0000313|Proteomes:UP000028641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH1 {ECO:0000313|EMBL:KFC24415.1,
RC ECO:0000313|Proteomes:UP000028641};
RA Pipes S.E., Stropko S.J.;
RT "Epilithonimonas sp. FH1 Genome.";
RL Submitted (JUL-2014) 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 -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|PIRNR:PIRNR001563}.
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:KFC24415.1}.
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DR EMBL; JPLZ01000002; KFC24415.1; -; Genomic_DNA.
DR RefSeq; WP_034963974.1; NZ_JPLZ01000002.1.
DR AlphaFoldDB; A0A085BPM0; -.
DR STRING; 1233951.IO90_03740; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000028641; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Ligase {ECO:0000256|PIRNR:PIRNR001563};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Reference proteome {ECO:0000313|Proteomes:UP000028641}.
FT DOMAIN 54..231
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 413 AA; 47004 MW; E79E895424B93F0F CRC64;
MNSHEYQKAV DWLFAQAPNY QRDGSSAYKP GLENIKKLCD FFGNPQDIIK TIHIGGTNGK
GSTSNMLASV LQESDYNVGL YNSPHLVDFT ERIKVNGKNC DKEFVYDFIQ KLKELPSEIQ
PSFFEFTTIM AFEYFYQQKV DYAIIEVGLG GRLDSTNIIK PTVSAITNVQ LDHQDLLGET
IEEIAFEKAG IIKENIPIIS GDEKTSVHDI IINKAEKMNA KFIDATTIET SLESDLKGKY
QKKNIRVVLA LVDELRRQNL TITKENIKSG LQNVYKNTNF IGRWFEFSQN PLTICDTGHN
KAGLEEVFNQ LNDYSQHKHI VLGFVNDKKI DEVLEILPKN ENYYFVKPNV NRGRNPETYE
HLLKKSEINY KIFQNVQDGY LSATQNCKAG EMIFIGGSNF VVGDFLEKNL LTS
//
