ID A0A1B1NAP6_9MICO Unreviewed; 492 AA.
AC A0A1B1NAP6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SGUI_1095 {ECO:0000313|EMBL:ANS78491.1};
OS Serinicoccus hydrothermalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=1758689 {ECO:0000313|EMBL:ANS78491.1, ECO:0000313|Proteomes:UP000092482};
RN [1] {ECO:0000313|EMBL:ANS78491.1, ECO:0000313|Proteomes:UP000092482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT9 {ECO:0000313|EMBL:ANS78491.1,
RC ECO:0000313|Proteomes:UP000092482};
RA Tang K.;
RT "Shallow-sea hydrothermal system.";
RL Submitted (MAR-2016) 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; CP014989; ANS78491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1NAP6; -.
DR STRING; 1758689.SGUI_1095; -.
DR KEGG; serj:SGUI_1095; -.
DR PATRIC; fig|1758689.4.peg.1133; -.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000092482; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ANS78491.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092482}.
FT DOMAIN 180..325
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 351..426
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 52112 MW; 3DEE4C7739538CBB CRC64;
MSDNFFEGED GSTELPLDPG SAVPTAEVTS LSGRGGTETT DPALLARYAE VSEAILARTP
EHMPQPTLHR VARVMELMGD PQRSFRMIHL TGTNGKTSTA RITERLLREM GLRTGRFTSP
HLHDMRERVS IDGRPVSIEA FLAAYDDVLP FVEMVDAESM ESPDEADRVR MTYFEVIVAL
AYAAFAAAPV EVAVVEVGLG GVWDATSVAD GDVAVLTPVA LDHTRLLGST LEEIATEKAG
IIKPDAIAVV GVQEPEVMQV LTDRAEEVGA QLRAEGVAFG VLAREVAVGG QQLSVRGLAG
DYPDLFLPLF GAYQAHNATL AIAAVEAFVG GGEQPLSDEV LRAGLAEVSS PGRLEIVRRS
PTVLVDAAHN PAGVEALVEA VRESFTFTRL VGLLAVLEDK DAEQMIQALE PVLDHVVVSR
TTSPRAIRPQ RLGELVAEFF GEDRVTVVAD LPDALDVAAG LADDGGVGGA VLATGSVTTA
AEVRELLGQR SA
//
