ID FTHS_MOOTH Reviewed; 559 AA. AC P21164; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 08-NOV-2023, entry version 110. 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}; OS Moorella thermoacetica (Clostridium thermoaceticum). OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella. OX NCBI_TaxID=1525; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2200509; DOI=10.1021/bi00476a007; RA Lovell C.R., Przybyla A., Ljungdahl L.G.; RT "Primary structure of the thermostable formyltetrahydrofolate synthetase RT from Clostridium thermoaceticum."; RL Biochemistry 29:5687-5694(1990). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT. RX PubMed=10747779; DOI=10.1021/bi992790z; RA Radfar R., Shin R., Sheldrick G.M., Minor W., Lovell C.R., Odom J.D., RA Dunlap R.B., Lebioda L.; RT "The crystal structure of N(10)-formyltetrahydrofolate synthetase from RT Moorella thermoacetica."; RL Biochemistry 39:3920-3926(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MONOVALENT CATIONS. RX PubMed=11087401; DOI=10.1021/bi001577w; RA Radfar R., Leaphart A., Brewer J.M., Minor W., Odom J.D., Dunlap R.B., RA Lovell C.R., Lebioda L.; RT "Cation binding and thermostability of FTHFS monovalent cation binding RT sites and thermostability of N10-formyltetrahydrofolate synthetase from RT Moorella thermoacetica."; RL Biochemistry 39:14481-14486(2000). CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216; CC EC=6.3.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01543}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_01543}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10747779, CC ECO:0000269|PubMed:11087401}. CC -!- MISCELLANEOUS: Binding of monovalent cations contributes to thermal CC stability. 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; J02911; AAA23240.1; -; Genomic_DNA. DR PIR; A35942; A35942. DR PDB; 1EG7; X-ray; 2.50 A; A/B=1-559. DR PDB; 1FP7; X-ray; 3.20 A; A/B=1-559. DR PDB; 1FPM; X-ray; 3.00 A; A/B=1-559. DR PDB; 3QUS; X-ray; 2.84 A; A/B=1-559. DR PDB; 4JIM; X-ray; 2.20 A; A/B=1-559. DR PDB; 4JJK; X-ray; 3.00 A; A/B=1-559. DR PDB; 4JJZ; X-ray; 2.50 A; A/B=1-559. DR PDB; 4JKI; X-ray; 2.67 A; A/B=1-559. DR PDBsum; 1EG7; -. DR PDBsum; 1FP7; -. DR PDBsum; 1FPM; -. DR PDBsum; 3QUS; -. DR PDBsum; 4JIM; -. DR PDBsum; 4JJK; -. DR PDBsum; 4JJZ; -. DR PDBsum; 4JKI; -. DR AlphaFoldDB; P21164; -. DR SMR; P21164; -. DR BioCyc; MetaCyc:FORMYLSYNTHCLTH-MONOMER; -. DR BRENDA; 6.3.4.3; 1528. DR UniPathway; UPA00193; -. DR EvolutionaryTrace; P21164; -. 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1. DR Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00722; FTHFS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; KW One-carbon metabolism. FT CHAIN 1..559 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_0000199361" FT BINDING 68..75 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" FT HELIX 19..24 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 46..51 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 58..66 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 74..87 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 122..126 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 127..130 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 132..152 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 168..172 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 178..183 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:3QUS" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 204..211 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 215..223 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 226..230 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 244..250 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 251..255 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 258..262 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 267..270 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 276..279 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 285..294 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 296..304 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 306..308 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 309..315 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 317..321 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 334..339 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 340..342 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 353..371 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 372..374 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 377..382 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 389..398 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 399..401 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 402..407 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 412..414 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 415..419 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 420..432 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 443..445 FT /evidence="ECO:0007829|PDB:1FP7" FT HELIX 447..457 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 462..466 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 468..479 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 480..484 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 487..490 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 495..498 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 510..513 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 517..519 FT /evidence="ECO:0007829|PDB:1EG7" FT TURN 520..522 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 523..527 FT /evidence="ECO:0007829|PDB:1EG7" FT HELIX 543..545 FT /evidence="ECO:0007829|PDB:1EG7" FT STRAND 551..555 FT /evidence="ECO:0007829|PDB:1EG7" SQ SEQUENCE 559 AA; 59993 MW; 36CD2BBB3C909B62 CRC64; MSKVPSDIEI AQAAKMKPVM ELARGLGIQE DEVELYGKYK AKISLDVYRR LKDKPDGKLI LVTAITPTPA GEGKTTTSVG LTDALARLGK RVMVCLREPS LGPSFGIKGG AAGGGYAQVV PMEDINLHFT GDIHAVTYAH NLLAAMVDNH LQQGNVLNID PRTITWRRVI DLNDRALRNI VIGLGGKANG VPRETGFDIS VASEVMACLC LASDLMDLKE RFSRIVVGYT YDGKPVTAGD LEAQGSMALL MKDAIKPNLV QTLENTPAFI HGGPFANIAH GCNSIIATKT ALKLADYVVT EAGFGADLGA EKFYDVKCRY AGFKPDATVI VATVRALKMH GGVPKSDLAT ENLEALREGF ANLEKHIENI GKFGVPAVVA INAFPTDTEA ELNLLYELCA KAGAEVALSE VWAKGGEGGL ELARKVLQTL ESRPSNFHVL YNLDLSIKDK IAKIATEIYG ADGVNYTAEA DKAIQRYESL GYGNLPVVMA KTQYSFSDDM TKLGRPRNFT ITVREVRLSA GGRLIVPITG AIMTMPGLPK RPAACNIDID ADGVITGLF //