ID A0A2N0VKQ1_9BACT Unreviewed; 427 AA.
AC A0A2N0VKQ1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=CWD77_04710 {ECO:0000313|EMBL:PKD44768.1};
OS Rhodohalobacter barkolensis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2053187 {ECO:0000313|EMBL:PKD44768.1, ECO:0000313|Proteomes:UP000233398};
RN [1] {ECO:0000313|EMBL:PKD44768.1, ECO:0000313|Proteomes:UP000233398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15182 {ECO:0000313|EMBL:PKD44768.1,
RC ECO:0000313|Proteomes:UP000233398};
RA Han S.;
RT "Rhodohalobacter 15182 sp. nov., isolated from a salt lake.";
RL Submitted (NOV-2017) 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 -!- 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:PKD44768.1}.
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DR EMBL; PISP01000001; PKD44768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0VKQ1; -.
DR Proteomes; UP000233398; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR001563};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233398}.
FT DOMAIN 52..244
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 427 AA; 48752 MW; 0A11695842A1108E CRC64;
MFDTIEEVES YMLSIPKFGT VGRSAANFNL DRMKEFCETM GNPQERVPMI HVAGTNGKGT
TCQMLASVYQ EAGYRVGLYT SPHLVDVRER FRINGEWITD SYFLEFFQEY GEFILSRKVT
FFELTTAIAF WYYERQDVDL AVIETGLGGR LDATNVIDPL VSVITSVGMD HTDILGDSIA
KIAEEKAGII KNNRPIVVGR LDKEAVSVIN DIAEKKGANV HHATKLNPEY ENDNFILHVE
SGKVSINAEG RKQIDAINVA VSWCVRELLQ AEFEVSEASF IAGIEKMDSR IGYHAHFYKI
HPVNKWYFDG AHNVESVIEL IKELKRIAPP QKWRVILSFM DDKLRQEISN LWNEFPNLMI
YQQEGDRAAS VEKMKSYFPK AEVVTSEQAI QYFGAEDKKT ELVIFSGSFY FYKTVRNWMG
TEAYNHT
//
