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Database: UniProt
Entry: A0A0S9Q2U1_9ACTN
LinkDB: A0A0S9Q2U1_9ACTN
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ID   A0A0S9Q2U1_9ACTN        Unreviewed;       479 AA.
AC   A0A0S9Q2U1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=ASF47_09310 {ECO:0000313|EMBL:KQP64206.1};
OS   Nocardioides sp. Leaf285.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP64206.1, ECO:0000313|Proteomes:UP000051495};
RN   [1] {ECO:0000313|EMBL:KQP64206.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP64206.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP64206.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP64206.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:KQP64206.1}.
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DR   EMBL; LMNH01000003; KQP64206.1; -; Genomic_DNA.
DR   RefSeq; WP_056863748.1; NZ_LMNH01000003.1.
DR   AlphaFoldDB; A0A0S9Q2U1; -.
DR   Proteomes; UP000051495; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051495}.
FT   DOMAIN          142..286
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          311..386
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   479 AA;  50354 MW;  58D0B7904A825522 CRC64;
     MTQTPATPDV PRLAETFSEV EDALLSRWPE TRLEPSLDRI AAFTELLGEP QRSYPVVHLT
     GTNGKTSTSR MIDTLLRTLD LRTGRFTSPH VERMNERISI DGEPLDDEAF VRAFNDVAPY
     THLVDEDQLH PLSFFETVVG MAFAAFADAP VEVAVLEVGM GGAWDATNVA DAAVAVVLPV
     AVDHAKYLGD RPDTIAAEKA GIIKAGSRVV LAQQTPEAAA VLLARAAEVG AEVVQEGLDF
     GVAARTPAVG GQVLSLQGLR ARYDDVFLPL HGAHQAQNAA VALAAVESFV GGEQPLDADL
     VGAAFAEVTS PARLEVVRRS PTIVLDAAHN PHGAEALAAA LDDSFTFSPL IGVVGVMGDK
     DAEGLLSALE PHLSHVVCTQ SSTDRALPAE DLAEIARGIF DDDQVTVVPR LAEALDAAAA
     LAEAGEAFGD PLGSGAVLVT GSVVTAGEAR GLLVSERGTQ AQRVARREID QQLEQGDDQ
//
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