ID A6D0N3_9VIBR Unreviewed; 426 AA.
AC A6D0N3;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Dihydrofolate synthase/folylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00019357};
DE EC=6.3.2.12 {ECO:0000256|ARBA:ARBA00013023};
DE EC=6.3.2.17 {ECO:0000256|ARBA:ARBA00013025};
DE AltName: Full=Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase {ECO:0000256|ARBA:ARBA00032510};
DE AltName: Full=Folylpolyglutamate synthetase {ECO:0000256|ARBA:ARBA00030048};
DE AltName: Full=Tetrahydrofolylpolyglutamate synthase {ECO:0000256|ARBA:ARBA00030592};
GN ORFNames=VSAK1_10128 {ECO:0000313|EMBL:EDL53786.1};
OS Vibrio mediterranei AK1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL53786.1, ECO:0000313|Proteomes:UP000003769};
RN [1] {ECO:0000313|EMBL:EDL53786.1, ECO:0000313|Proteomes:UP000003769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EDL53786.1,
RC ECO:0000313|Proteomes:UP000003769};
RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in two distinct reactions of the de novo folate
CC biosynthetic pathway. Catalyzes the addition of a glutamate residue to
CC dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate
CC (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes
CC successive additions of L-glutamate to tetrahydrofolate or 10-
CC formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to
CC folylpolyglutamate derivatives. {ECO:0000256|ARBA:ARBA00002714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-
CC glutamate = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:51912, Rhea:RHEA-COMP:13257,
CC Rhea:RHEA-COMP:13258, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:136572,
CC ChEBI:CHEBI:456216; EC=6.3.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000809};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=10-formyltetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate
CC = 10-formyltetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:51904, Rhea:RHEA-COMP:13088, Rhea:RHEA-
CC COMP:14300, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:134413, ChEBI:CHEBI:456216;
CC EC=6.3.2.17; Evidence={ECO:0000256|ARBA:ARBA00000058};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216;
CC EC=6.3.2.12; Evidence={ECO:0000256|ARBA:ARBA00000104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004799}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005150}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:EDL53786.1}.
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DR EMBL; ABCH01000013; EDL53786.1; -; Genomic_DNA.
DR RefSeq; WP_006071326.1; NZ_ABCH01000013.1.
DR AlphaFoldDB; A6D0N3; -.
DR UniPathway; UPA00077; UER00157.
DR Proteomes; UP000003769; 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:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR018109; Folylpolyglutamate_synth_CS.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
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; PF02875; Mur_ligase_C; 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 Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
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 54..194
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 288..340
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 426 AA; 46529 MW; B345960DAD9367DF CRC64;
MSSQSIPQAT SSLQVWLDYL NSIHTSAIDL GLDRVSVVAQ KGQLTKPAPT VITVAGTNGK
GSTCALMEAI LLDAGYSVGV YSSPHLIRYN ERVRVNGSDL PDESHTRAFD YIEKLRGEVS
LSFFEYATLA ALRQFQENKV EVVLLEVGLG GRLDATNVVD HDVSVITSLA VDHVDWLGDD
INVIGFEKAG IFRTGKPAIC GQPKPPATVP AHADDIKANF YQSGIQFDYK LTSEHTWAWQ
HGTFMLEDLP VPVLPLMNAN TALMALGAAE LDISDVNIVN GLKQARLPGR MQMLTGSPVT
ILDVAHNPHS AEYLVAQLSK HYPNRRFKVV IGMLHDKDIE ETIRVLNPLT EDWYPASLSG
PRAASADELC QHLMSGNALK QYDNPVSAYQ AAKSEAKSDD MILVVGSFHT VGEVLEHCEK
LDAQEQ
//
