FTHS_STRSY
ID FTHS_STRSY Reviewed; 556 AA.
AC A4VU67;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=SSU05_0690;
OS Streptococcus suis (strain 05ZYH33).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=391295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05ZYH33;
RX PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA Yang R., Wang J., Yu J.;
RT "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT of S. suis 2 Chinese isolates.";
RL PLoS ONE 2:E315-E315(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR EMBL; CP000407; ABP89656.1; -; Genomic_DNA.
DR AlphaFoldDB; A4VU67; -.
DR SMR; A4VU67; -.
DR STRING; 391295.SSU05_0690; -.
DR EnsemblBacteria; ABP89656; ABP89656; SSU05_0690.
DR KEGG; ssu:SSU05_0690; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000243; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00477; FTHFS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01543; FTHFS; 1.
DR InterPro; IPR000559; Formate_THF_ligase.
DR InterPro; IPR020628; Formate_THF_ligase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01268; FTHFS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300548"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 59108 MW; 6CC2ED05FD864616 CRC64;
MKTDIDIAQS ITLKPITEIV EKVGISFDDI ELYGKYKAKL SFDKINAVKD NAPGKLILVT
AINPTPAGEG KSTITIGLAD ALSKIGKKTM IALREPSLGP VMGIKGGAAG GGYAQVLPME
DINLHFTGDM HAITTANNAL SALIDNHIHQ GNVIGIDQRR IIWKRVVDLN DRALRKVTVG
LGGPLNGIPR EDGFDITVAS EIMAILCLAT DINDLKERLA NIVIGYRFDC SPVYVRDLAV
EGALTLILKD AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATTTALR LADYTVTEAG
FGADLGAEKF LDIKVPNLPK APDAVVIVAT LRALKMHGGV AKTELSAENV EAVKAGFSNL
KRHVENIRKY GIPAVVAINE FVSDTAAEIA VLKELCAAIG VPVELASVWA NGADGGVELA
ETVVATIDNQ AASYQRLYKS EDSLEEKVTK IVTQIYGGTG VVFEKKARNQ LTEFAKNGWD
KLPVCMAKTQ YSFSDDQFAL GAPTDFDITV REFVPKLGAG FIVALTGDVM TMPGLPKAPV
ALNMDVAADG TAIGLF
