FTHS2_STRP3
ID FTHS2_STRP3 Reviewed; 557 AA.
AC P0DF92; Q79W25; Q8K5L8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Formate--tetrahydrofolate ligase 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS 2 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS 2 {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs2 {ECO:0000255|HAMAP-Rule:MF_01543}; Synonyms=fhs.2;
GN OrderedLocusNames=SpyM3_1776;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(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; AE014074; AAM80383.1; -; Genomic_DNA.
DR RefSeq; WP_011055075.1; NC_004070.1.
DR AlphaFoldDB; P0DF92; -.
DR SMR; P0DF92; -.
DR EnsemblBacteria; AAM80383; AAM80383; SpyM3_1776.
DR GeneID; 57853439; -.
DR KEGG; spg:SpyM3_1776; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; TRQGFSK; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000564; 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..557
FT /note="Formate--tetrahydrofolate ligase 2"
FT /id="PRO_0000199396"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 59052 MW; 029820DF95BB401A CRC64;
MVLSDIEIAN SVTMEPISKV ANQLGIDEEA LCLYGKYKAK IDARQLVALK DKPDGKLILV
TAISPTPAGE GKTTTSVGLV DALSAIGKKA VIALREPSLG PVFGVKGGAA GGGHAQVVPM
EDINLHFTGD FHAIGVANNL LAALIDNHIH HGNSLGIDSR RITWKRVVDM NDRQLRHIVD
GLQGKVNGAP REDGYDITVA SEIMAILCLS ENISDLKARL EKIIIGYNYR GEPVTAKDLK
AGGALAALLK DAIHPNLVQT LEHTPALIHG GPFANIAHGC NSVLATKLAL KYGDYAVTEA
GFGADLGAEK FIDIKCRMSG LRPAAVVLVA TIRALKMHGG VPKADLATEN VQAVVDGLPN
LDKHLANIQD VYGLPVVVAI NKFPLDTDAE LQAVYDACDK RGVDVVISDV WANGGAGARE
LAEKVVTLAE QDNQFRFVYE EDDSIETKLT KIVTKVYGGK GITLSPAAKR ELADLERLGF
GNYPICMAKT QYSFSDDAKK LGAPTDFTVT ISNLKVSAGA GFIVALTGAI MTMPGLPKVP
ASETIDIDEE GNITGLF