ID K8Z876_9ENTE Unreviewed; 436 AA.
AC K8Z876;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=C683_0565 {ECO:0000313|EMBL:EKU27234.1};
OS Catellicoccus marimammalium M35/04/3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Catellicoccus.
OX NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU27234.1, ECO:0000313|Proteomes:UP000016057};
RN [1] {ECO:0000313|EMBL:EKU27234.1, ECO:0000313|Proteomes:UP000016057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU27234.1,
RC ECO:0000313|Proteomes:UP000016057};
RX PubMed=23405330;
RA Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., Santo Domingo J.W.;
RT "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT Commonly Found in Gull Feces.";
RL Genome Announc. 1:E00019-12(2013).
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 -!- 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:EKU27234.1}.
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DR EMBL; AMYT01000017; EKU27234.1; -; Genomic_DNA.
DR RefSeq; WP_009489719.1; NZ_AMYT01000017.1.
DR AlphaFoldDB; K8Z876; -.
DR STRING; 1234409.C683_0565; -.
DR PATRIC; fig|1234409.3.peg.515; -.
DR eggNOG; COG0285; Bacteria.
DR OrthoDB; 9809356at2; -.
DR Proteomes; UP000016057; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001563};
KW Ligase {ECO:0000256|PIRNR:PIRNR001563, ECO:0000313|EMBL:EKU27234.1};
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:UP000016057}.
FT DOMAIN 44..272
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 300..375
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 436 AA; 49548 MW; 5892AAA93CD3DAA3 CRC64;
MDVYTAINWI HERKKFSKNP NLTRVQHLLH QLGNPERDLK VIHVAGTNGK GSTVAYLSAL
FQELNYTVGS FTSPYIESFN ERICLNGRPI SDTELIALIC RIQPLVKEMD EIEDLQGCTE
FEITTAMMFC YFKEKGVDIA LIEVGLGGMY DSTNVVCKPL VTGISSIGYD HMQLLGDTLE
EIASEKMGIF KPNCPVVLGK MEECIENYCT DYALSLKCPV YRYNTEYRVD YLGRSSKKVG
EKFNYKDNMR SAKRLVTPLI GHHQVENASF ALQIFDIALH YEKRTLSNND VQHALAKVNW
PGRMEIYQNE PLIILDGAHN APAMKRLVET LEDEYKDYEV HVLFSALQGK QYPEMIAELQ
KLPNVDITLT TFDTPKALPI EAFESYREGG LTVTDNWKKA FFDLLKGMDD SKEMVVVTGS
LYFLSQVRNF LMSGIV
//
