FTHS1_STRP8
ID FTHS1_STRP8 Reviewed; 556 AA.
AC Q8P0X5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Formate--tetrahydrofolate ligase 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS 1 {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs1 {ECO:0000255|HAMAP-Rule:MF_01543}; Synonyms=fhs;
GN OrderedLocusNames=spyM18_1165;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
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; AE009949; AAL97781.1; -; Genomic_DNA.
DR RefSeq; WP_011017800.1; NC_003485.1.
DR AlphaFoldDB; Q8P0X5; -.
DR SMR; Q8P0X5; -.
DR KEGG; spm:spyM18_1165; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
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.
FT CHAIN 1..556
FT /note="Formate--tetrahydrofolate ligase 1"
FT /id="PRO_0000199391"
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; 59503 MW; DBC6D12168F0C3F8 CRC64;
MKSDIEIAQS VALQPITDIV KKVGIDGDDI ELYGKYKAKL SFEKMKAVEA NEPGKLLLVT
AINPTPAGEG KSTMSIGLAD ALNQMGKKTM LALREPSLGP VMGIKGGAAG GGYAQVLPME
DINLHFTGDM HAITTANNAL SALIDNHLQQ GNDLGIDPRR IIWKRVLDLN DRALRQVIVG
LGSPVNGVPR EDGFDITVAS EIMAILCLAT DLKDLKKRLA DIVVAYTYDR KPVYVRDLKV
EGALTLILKD AIKPNLVQTI YGTPALIHGG PFANIAHGCN SVLATSTALR LADYTVTEAG
FGADLGAEKF LNIKVPNLPK APDAIVIVAT LRALKMHGGV AKSDLAAENC EAVRLGFANL
KRHVENMRQF KVPVVVAINE FVADTEAEIA TLKALCEEIK VPVELASVWA NGAEGGLALA
KTAVRVIDQE AADYKRLYSD EDTLEEKVIN IVTQIYGGKA VQFGPKAKTQ LKQFAEFGWD
KLPVCMAKTQ YSFSDNPSLL GAPTDFDITI REFVPKTGAG FIVGLTGDVM TMPGLPKVPA
AMAMDVAENG TALGLF