FTHS_STAHJ
ID FTHS_STAHJ Reviewed; 555 AA.
AC Q4L776;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=SH1190;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04499.1; -; Genomic_DNA.
DR RefSeq; WP_011275491.1; NC_007168.1.
DR AlphaFoldDB; Q4L776; -.
DR SMR; Q4L776; -.
DR STRING; 279808.SH1190; -.
DR EnsemblBacteria; BAE04499; BAE04499; SH1190.
DR GeneID; 58062608; -.
DR KEGG; sha:SH1190; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000543; 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..555
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199383"
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; 59718 MW; 4F158417D278407C CRC64;
MAHLSDLDIA NQSELKPIGE IAEKAGIPAD ALEQYGHYKA KIDINQIKPK DNKGKVVLVT
AMSPTPAGEG KSTVTVGLSD AFNELKKNVM VALREPALGP TFGIKGGATG GGYAQVLPME
DINLHFNGDF HAITTANNAL SAFIDNHIHQ GNELGIDVRR VEWKRVLDMN DRALRHVNVG
LGGPTNGVPR EDGFNITVAS EVMAILCLAR NINDLKEKIS RITIGYTRDR KPVTVADLKV
EGALAMILKD AIKPNLVQTI EGTPALVHGG PFANIAHGCN SILATETARD LADIVVTEAG
FGSDLGAEKF IDIKAREAGF EPSAVVLVAT VRALKMHGGV AKDDLKEENV EAVKAGIVNL
ERHVNNIRKF GVEPVIALNA FIHDTDAETE AVKAWAKENN VRIALTEVWE KGGKGGVELA
NQVLEVIEQP NDFKFLYDLD QSLEEKIETI VKDIYGGSSV TFSKKAKKQL KEFTDNGWGQ
YPICMAKTQY SFSDDATALG APTDFDITIR ELEAKTGAGF IVALTGAIMT MPGLPKKPAA
LNMDVTEDGH AVGLF
