ID F3Z8M1_9ACTN Unreviewed; 506 AA.
AC F3Z8M1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=STTU_4618 {ECO:0000313|EMBL:EGJ77407.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ77407.1};
RN [1] {ECO:0000313|EMBL:EGJ77407.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ77407.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CM001165; EGJ77407.1; -; Genomic_DNA.
DR RefSeq; WP_007827101.1; NZ_CM001165.1.
DR AlphaFoldDB; F3Z8M1; -.
DR HOGENOM; CLU_015869_1_2_11; -.
DR Proteomes; UP000003955; 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 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 108..335
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 364..444
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 54010 MW; 7ABF7F8BA8167811 CRC64;
MSEQPPHDDR TDGDDEHFDR IIDAETERDP DLAVIEAGSR TLRAQAGPPQ ADVPARPEDP
EVDRALREVE TELSTRWGET KLEPSVSRIA ALMDVLGEPQ RSYPSIHITG TNGKTSTARM
IEALLTAFDL RTGRYTSPHV QSITERISLD GAPISAERFI ETYRDLKPYI EMVDSRQEYR
LSFFEVLTGM AYAAFADAPA DVAVVEVGMG GSWDATNVID ADVAVITPIS LDHTDRLGNT
PGEIAVEKSG IIKQDATVVL SQQPVDAAQV ILKKAVERNA TVAREGMEFG VVSRQVAVGG
QLLTLRGLGG EYEEIFLPLH GAHQAHNAAV ALAAVEAFFG VGSQRPEPLS GEVVRAAFAA
VSSPGRLETV RKSPTVVVDA AHNPAGARVT AEAIGEAFDF SRLIGVVGVS EGKDARGLLE
AFEPIMAEVV ITQNTSHRAM DADALAALAV EVFGEDRVQV EPRLPEALEA AVTLAEEEGE
FAGGGVLVTG SVITVGEARL LLGRKG
//
