FTHS_MOOTH
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 03-AUG-2022, entry version 105.
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; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; 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 = (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 -!- 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}.
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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-MON; -.
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; 3.40.50.300; -; 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 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
