FTHS_THET2
ID FTHS_THET2 Reviewed; 543 AA.
AC Q72GY9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=TT_C1707;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017221; AAS82049.1; -; Genomic_DNA.
DR RefSeq; WP_011174070.1; NC_005835.1.
DR AlphaFoldDB; Q72GY9; -.
DR SMR; Q72GY9; -.
DR STRING; 262724.TT_C1707; -.
DR PRIDE; Q72GY9; -.
DR EnsemblBacteria; AAS82049; AAS82049; TT_C1707.
DR KEGG; tth:TT_C1707; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_0; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000592; 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..543
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199404"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 543 AA; 58348 MW; 09FCE0CBF76D665E CRC64;
MIVKEDLLPI EEVAAKLGLD RDRLYLYGPH MAKVLGEPPK AKGKLVLVTA ITPTPAGEGK
TTTAIGLVDA LWRLGKRAAL ALREPSLGPV FGVKGGATGG GKARVEPRHE INLHFTGDFH
AVTSAVNLLN ALLDNHLHQG NELGIDPRRI ELKRAIDMND RALRHIVLGL GGKAHGVPRE
GGFELTVASE VMALMSLARD FQDLKRRLGR MRVAFTHEGK PVYAEDLMAV GAMAALLRQA
FLPNLVQTAE GNPAFIHMGP FGNIAHGTNS LRASLFALGL ADLVVQEAGF ATDLGLEKFM
NVVARTTGLV PEAVVLVATI RALRYHGGQD AYGMPDPKAV KAGLANLEKH VENVELFGYK
PVIALNRFPS DAPEEIALVR AFAEERGLPF APSEVYAQGG EGGLELAERV LEALDLPHAY
RPLYPLEASL EAKVEAIATR VYGAEGVEWS EEAKRALKAA KKEGCEALPV VVAKAATSLS
DNPRLRGRPR GFTVRVTDLR CRLGAGFVVV YMGGIETLPG LPKTPQAFGI DVDEEGNIRG
MDY
