ID A0A372NZV3_9SPHI Unreviewed; 434 AA.
AC A0A372NZV3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D0C36_06640 {ECO:0000313|EMBL:RFZ95199.1};
OS Mucilaginibacter conchicola.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2303333 {ECO:0000313|EMBL:RFZ95199.1, ECO:0000313|Proteomes:UP000264217};
RN [1] {ECO:0000313|EMBL:RFZ95199.1, ECO:0000313|Proteomes:UP000264217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYSH2 {ECO:0000313|EMBL:RFZ95199.1,
RC ECO:0000313|Proteomes:UP000264217};
RA Seo T.;
RT "Mucilaginibacter sp. MYSH2.";
RL Submitted (AUG-2018) 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:RFZ95199.1}.
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DR EMBL; QWDC01000001; RFZ95199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372NZV3; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000264217; 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}.
FT DOMAIN 51..278
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 434 AA; 47431 MW; BCD4B61318B19314 CRC64;
MNYNETLDYL YTQLPMFTRD GASAFKKDLT NTLALCVLLD NPQHKFKSVH VGGTNGKGST
SHMLAAILQV AGYKTGLYTS PHLRDFRERI RINGQMISEQ KVIDFVAANR KAFEDIQPSF
FEMTVALAFD VFAKEQVDIA VVEVGLGGRL DSTNVITPLL SVITNIGWDH MNMLGNTLEL
IAGEKAGIIK PGIPVVIGER QPEVADIFIQ KAGKEGSEIN FASDVKSIKL KAESPKSKEK
ELLDISVSSS GSGLQTLDLE LDLTGTYQLK NVKTVLTAVD ELRKQGFNIT DEHITTALKQ
VKTLTGLHGR WETLSTDPLT ICDTGHNPEG IQEVMKNIAS VNYDQLHFVI GMVNDKDSSK
VLSMLPKDAT YYFCKPDIPR GLDATSLQEQ AAAFDLTGQT YSTVKTAYEA AQQAAGKNDL
VFVGGSTFVV AEVV
//
