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Database: UniProt
Entry: A0A1K1M132_9FIRM
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Original site: A0A1K1M132_9FIRM 
ID   A0A1K1M132_9FIRM        Unreviewed;       556 AA.
AC   A0A1K1M132;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000256|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000256|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000256|HAMAP-Rule:MF_01543};
GN   Name=fhs {ECO:0000256|HAMAP-Rule:MF_01543};
GN   ORFNames=SAMN02910447_00588 {ECO:0000313|EMBL:SFW16861.1};
OS   Ruminococcus sp. YE71.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=244362 {ECO:0000313|EMBL:SFW16861.1, ECO:0000313|Proteomes:UP000182164};
RN   [1] {ECO:0000313|EMBL:SFW16861.1, ECO:0000313|Proteomes:UP000182164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE71 {ECO:0000313|EMBL:SFW16861.1,
RC   ECO:0000313|Proteomes:UP000182164};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|HAMAP-Rule:MF_01543}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01543}.
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DR   EMBL; FPIR01000002; SFW16861.1; -; Genomic_DNA.
DR   RefSeq; WP_072416711.1; NZ_FPIR01000002.1.
DR   AlphaFoldDB; A0A1K1M132; -.
DR   STRING; 244362.SAMN02910447_00588; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000182164; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01543, ECO:0000313|EMBL:SFW16861.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01543}; Reference proteome {ECO:0000313|Proteomes:UP000182164}.
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   556 AA;  59385 MW;  A178B9E9C5624434 CRC64;
     MLTDIEIAQQ AKMLRIGEIA KSLGIAEEDF EPYGHYKAKL SEQLYVKTAD KPDGKLILVT
     AINPTPAGEG KTTVSVGLAE GMAKTGRNAI LALREPSLGP VFGIKGGAAG GGYAQVVPMD
     DINLHFTGDM HAITAANNLL CALIDNHIHQ GNVLRIDQRR ILFKRCMDMN DRALRSVIVG
     LGGKVNGFPR EDGFQITVAS EIMAILCLAA DLADLKARLE RILVGYDLDG NPVYAGQLQG
     CGAMAALLKD ALKPNLVQTL ENTPAIMHGG PFANIAHGCN SVRATKLCLK LADYTITEAG
     FGSDLGAEKF FDIKCRYAGL KPNCVVLVAT IRALKYNGGV ARADLKTENV EALKKGSVNL
     RTHIENMQKF GVPVVVAINR FADDTDAEIA VIEEVCSQCG VEFSLTEVFA KGGEGAADLA
     DKVVNAIETK PSQYKPLYDT ALPVKEKIGT IAREIYRADG VIYTAQAEKA LKEIEALGKT
     DLPICVAKTQ YSLSDDPTKL GKPEGFEITV RDMKLSSGAG FIVVYTGDIM TMPGLPKAPA
     ANNIDVDNAG NISGLF
//
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