ID A0A0P7WVK8_9GAMM Unreviewed; 430 AA.
AC A0A0P7WVK8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:KPQ04678.1};
GN ORFNames=HLUCCO02_12050 {ECO:0000313|EMBL:KPQ04678.1};
OS Idiomarinaceae bacterium HL-53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae.
OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ04678.1, ECO:0000313|Proteomes:UP000053932};
RN [1] {ECO:0000313|EMBL:KPQ04678.1, ECO:0000313|Proteomes:UP000053932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ04678.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
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 -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
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:KPQ04678.1}.
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DR EMBL; LIHO01000007; KPQ04678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WVK8; -.
DR STRING; 1298881.Ga0003345_2395; -.
DR PATRIC; fig|1298881.4.peg.2498; -.
DR UniPathway; UPA00077; UER00157.
DR Proteomes; UP000053932; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008841; F:dihydrofolate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001563};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
FT DOMAIN 55..194
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 430 AA; 46993 MW; 42598C06AA5E196D CRC64;
MNLKHTQKPE PRSLDAWLSY LEQIHTKTID LGLERVEKVA QAMNVLQPAP YIILVGGTNG
KGSTVAMLNA ILTAHGLRTA TYTSPHLVNY RERVTVAGQW LSEAQHCEAF ARVEQVRKET
SLTYFEFGTL AALELIKNAQ VDVAILEIGL GGRLDAVNIV PPDLSIVTSV GIDHIAFLGD
DREVIGFEKA GIYRANKPAV CGDLHAPAAL VEFAERTGAQ LALAGIDFEI LSENETEWSL
RLPKGKLLEH LPKPHLPLQN AATALTALSL TPFALTQNDY TEGLMRAFVP GRFESIRQAP
IVILDVGHNP HAAAYLNHQL TKLKRYRPGV GKIRAVCGML KDKDIRGTIE AISESIDLWY
FASLPSERGA SAAELAAELS NRAHFVQESS VAIAYKRALS EASEQDVILC FGSFLTITAI
YEVEGKVIRG
//
