FTHS_FINM2
ID FTHS_FINM2 Reviewed; 554 AA.
AC B0S0G1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=FMG_0461;
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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; AP008971; BAG07879.1; -; Genomic_DNA.
DR AlphaFoldDB; B0S0G1; -.
DR SMR; B0S0G1; -.
DR STRING; 334413.FMG_0461; -.
DR PRIDE; B0S0G1; -.
DR EnsemblBacteria; BAG07879; BAG07879; FMG_0461.
DR KEGG; fma:FMG_0461; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001319; 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..554
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000146683"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 554 AA; 60642 MW; F0846196F79BA3D2 CRC64;
MFMATDVEIA QKAKLEKISV IAEKMGLTEE DYEQYGRYKA KLDLNLFEKN KDKKDGKLIL
MTSINPTPTG EGKTTMNVGL AMGLNKIGKN AISVLREPSL GPNFGMKGGA AGGGYAQVVP
MDEINMHFTG DFHAITTANN LICAMMDNHI HQGNALNIDP KQILIKRCMD MNERELRDII
IGVGAKGNGV MRQDGFEITV ASEIMAILCL AKDLKDLKER VGNILIAFDK EGKPVYARDV
KADGAVALVM KEAIKPNLVQ TLEHTPAIIH GGPFANIAHG CNSLIATKLG LKLGDYVVTE
AGFGADLGAE KFFDIKCRND LHPNMVCIVA TIKALKHHGE AEDFKVENVE ALEKGYANLK
RHIENMKKYK VPVVVAINRF ATDTDAEIKK LTELVEADGT RAIFCDVWAK GGEGAKELAE
YVVENTKEEN DFEFLYDLEL PIKEKIEKIA KEIYRADGVE FSAKAKKKLK QIKELGLDNY
PVCMAKTQYS FSDNKKLIGA PTGFTITVSD FKISRGAGFV VALLGSVMTM PGLPKVPSAE
NCDVLDDGTV VGLF
