FTHS1_STRPF
ID FTHS1_STRPF Reviewed; 556 AA.
AC Q1J6F7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=MGAS10750_Spy1076;
OS Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370554;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10750;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000262; ABF38026.1; -; Genomic_DNA.
DR RefSeq; WP_011528670.1; NC_008024.1.
DR AlphaFoldDB; Q1J6F7; -.
DR SMR; Q1J6F7; -.
DR EnsemblBacteria; ABF38026; ABF38026; MGAS10750_Spy1076.
DR KEGG; spi:MGAS10750_Spy1076; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002434; 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.
FT CHAIN 1..556
FT /note="Formate--tetrahydrofolate ligase 1"
FT /id="PRO_0000293065"
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; 59589 MW; 3C305882C7464213 CRC64;
MKSDIEIAQS VALQPITDIV KKVGIDGDDI ELYGKYKAKL SFEKMKAVEA NEPGKLILVT
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 NGAEGGIALA
KTVVRVIDQE AADYKRLYSD EDTLEEKVIN IVTQIYDGKA VQFGPKAKTQ LKQFAEFGWD
KLPVCMAKTQ YSFSDNPSLL GAPTDFDITI REFVPKTGAG FIVGLTGDVM TMPGLPKVPA
AMAMDVAENG TALGLF