FTHS_STAA8
ID FTHS_STAA8 Reviewed; 555 AA.
AC Q2G296;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=SAOUHSC_01845;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (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; CP000253; ABD30912.1; -; Genomic_DNA.
DR RefSeq; WP_000149403.1; NZ_LS483365.1.
DR RefSeq; YP_500350.1; NC_007795.1.
DR AlphaFoldDB; Q2G296; -.
DR SMR; Q2G296; -.
DR STRING; 1280.SAXN108_1761; -.
DR EnsemblBacteria; ABD30912; ABD30912; SAOUHSC_01845.
DR GeneID; 3920524; -.
DR KEGG; sao:SAOUHSC_01845; -.
DR PATRIC; fig|93061.5.peg.1681; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:Q2G296; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..555
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300544"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 555 AA; 59856 MW; 8314C426AEFDF11A CRC64;
MTHLSDLDIA NQSTLQPIKD IAASVGISED ALEPYGHYKA KIDINKITPR ENKGKVVLVT
AMSPTPAGEG KSTVTVGLAD AFHELNKNVM VALREPALGP TFGIKGGATG GGYAQVLPME
DINLHFNGDF HAITTANNAL SAFIDNHIHQ GNELGIDQRR IEWKRVLDMN DRALRHVNVG
LGGPTNGVPR EDGFNITVAS EIMAILCLSR SIKDLKDKIS RITIGYTRDR KPVTVADLKV
EGALAMILKD AIKPNLVQSI EGTPALVHGG PFANIAHGCN SILATETARD LADIVVTEAG
FGSDLGAEKF MDIKAREAGF DPAAVVVVAT IRALKMHGGV AKDNLKEENV EAVKAGIVNL
ERHVNNIKKF GVEPVVAINA FIHDTDAEVE YVKSWAKENN VRIALTEVWE KGGKGGVDLA
NEVLEVIDQP NSFKPLYELE LPLEQKIEKI VTEIYGGSKV TFSSKAQKQL KQFKENGWDN
YPVCMAKTQY SFSDDQTLLG APSGFEITIR ELEAKTGAGF IVALTGAIMT MPGLPKKPAA
LNMDVTDDGH AIGLF