GenomeNet

Database: UniProt
Entry: A0A0N9NAG1_9ACTN
LinkDB: A0A0N9NAG1_9ACTN
Original site: A0A0N9NAG1_9ACTN 
ID   A0A0N9NAG1_9ACTN        Unreviewed;       469 AA.
AC   A0A0N9NAG1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=ACH46_08250 {ECO:0000313|EMBL:ALG84490.1};
OS   Gordonia phthalatica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG84490.1, ECO:0000313|Proteomes:UP000063789};
RN   [1] {ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA   Jin D., Kong X., Bai Z.;
RT   "Complete genome sequence and metabolic analysis of phthalate degradation
RT   pathway in Gordonia sp. QH-11.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALG84490.1, ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|EMBL:ALG84490.1,
RC   ECO:0000313|Proteomes:UP000063789};
RX   PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA   Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT   "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT   isolated from activated sludge.";
RL   Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP011853; ALG84490.1; -; Genomic_DNA.
DR   RefSeq; WP_062392477.1; NZ_CP011853.1.
DR   AlphaFoldDB; A0A0N9NAG1; -.
DR   STRING; 1136941.ACH46_08250; -.
DR   KEGG; goq:ACH46_08250; -.
DR   PATRIC; fig|1136941.3.peg.1678; -.
DR   OrthoDB; 9809356at2; -.
DR   Proteomes; UP000063789; Chromosome.
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; 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   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          56..296
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          323..403
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   469 AA;  49453 MW;  D8DF12FC9236032A CRC64;
     MSRVTDSDDD LAELHALEAE LDTRWPETKI EPSLTRITAL MELLGNPQHA YPSIHIAGTN
     GKTSVTRMID SLLQAFHRRT GRVTSPHLQL VTERIAIDGA PIPARTYVDT YRDIEPYITM
     VDDSSTESGG PRMSKFEVLT ALAYAAFAEA PVEVAVIETG MGGRWDATNV INSQVAVITP
     IAMDHADYLG DTLAAIAGEK AGIIKAGQPD RVIPMDPITV IAPQAPEVTD VLLRAAVEAG
     TIVARQDSEF TVVDAVTAVG GQMLTIRGLG GVYDEIFLPL HGAHQAQNAA LALAAVEAFF
     GAGADRQLDV EAVRLGFAAV ASPGRLERLR GAPSVFIDAA HNPHGARALA QALVSEFDFR
     RLIGVIGVLG DKDVRGVLTE LEPVLDVVVL TNNGSPRALD TDALADIANQ VFGEDRVVIE
     PFLPDAVEAA IALAEEADEN GSVSGAGVVI TGSVVTAGAA RTLFGKEPS
//
DBGET integrated database retrieval system