ID A0A0D6MW96_ACEAC Unreviewed; 443 AA.
AC A0A0D6MW96; A0A7G1M6R3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=Abac_018_031 {ECO:0000313|EMBL:GAN57618.1};
OS Acetobacter aceti NBRC 14818.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX NCBI_TaxID=887700 {ECO:0000313|EMBL:GAN57618.1, ECO:0000313|Proteomes:UP000032677};
RN [1] {ECO:0000313|EMBL:GAN57618.1, ECO:0000313|Proteomes:UP000032677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 14818 {ECO:0000313|EMBL:GAN57618.1,
RC ECO:0000313|Proteomes:UP000032677};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acetobacter aceti NBRC 14818.";
RL Submitted (NOV-2012) 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 -!- 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 -!- 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:GAN57618.1}.
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DR EMBL; BAMU01000018; GAN57618.1; -; Genomic_DNA.
DR RefSeq; WP_010665921.1; NZ_SLZP01000005.1.
DR AlphaFoldDB; A0A0D6MW96; -.
DR OrthoDB; 9809356at2; -.
DR UniPathway; UPA00077; UER00157.
DR Proteomes; UP000032677; 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; IPR036615; Mur_ligase_C_dom_sf.
DR NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 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|PIRNR:PIRNR001563};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}.
SQ SEQUENCE 443 AA; 46789 MW; 6D59B8C97B4B9FB3 CRC64;
MTDTPSPRKP ALGAEFTGRT GTVLERLNRL YPALIDLSLG RLETLLAKLG HPEQHLPSVI
HVAGTNGKGS TCANLRAIGE AAGWRVHVMS SPHLVDVTER FRVAGKLVSE EELVATLEEI
EQVNGGEPIT VFEVLTAAGF LLFSRHPAEL AVIEVGLGGR FDATNVLARP AACAITAISM
DHEAFLGSTL AAIAGEKAGI IKSDVPVVTG RQPQAVQNVL AMEADVKGAP LLLRDRDWEL
TRSADGLSLL YKDAKGALTL PLPALTGTHQ DDNAGLAVAT LRASGLAVPE SAWAGIAHTR
WPARLQKLEG VLAAQLPTGW ELWLDGGHNP GAGEALVPVL EQWSDRPLHI LVGMKQTKDA
SGFLAPLLEH ATSVYAVAEP DQHLALPVEA IVEASHGRAQ PGPDIATALA NLSGKEEKAA
RVLICGSLYL AGVVLKKDGW RAE
//
