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Database: UniProt
Entry: A0A101E865_9FIRM
LinkDB: A0A101E865_9FIRM
Original site: A0A101E865_9FIRM 
ID   A0A101E865_9FIRM        Unreviewed;       560 AA.
AC   A0A101E865;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=XD50_1255 {ECO:0000313|EMBL:KUK10503.1};
OS   Clostridia bacterium 41_269.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK10503.1, ECO:0000313|Proteomes:UP000053409};
RN   [1] {ECO:0000313|Proteomes:UP000053409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUK10503.1}.
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DR   EMBL; LGEZ01000013; KUK10503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101E865; -.
DR   STRING; 1635275.XD50_1255; -.
DR   PATRIC; fig|1635275.3.peg.974; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000053409; 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:KUK10503.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_01543}.
FT   BINDING         69..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   560 AA;  60680 MW;  856D386533D4BD72 CRC64;
     MERPIPSDIE IALKAKKKPI MEIAENLGIK GDDLELFGKY KAKVSLDLMK RLEKTPDGKL
     ILVTAITPTP AGEGKTTNSI GLTDALNRLG KKAVVALREP SLGPNFGIKG GAAGGGYSQV
     VPMEDINLHF TGDIHAVTYA HNLLAAMIDN HIHQGNELNI DPRKIVFRRV LDLNDRALRF
     VVCGLGGPKN GVPRETGFDI SVASEIMAIL CLSLNLEDLK ERMGRIVVGY TYDDKPVTAA
     QLEAHGAMAV LMKDAIKPNL VQTLENNPAF IHGGPFANIA HGCNSIIATK MALKLADYVV
     TEAGFGADLG AEKFFNLKCR YGGLRPSGVV VVASVRALKF HGGISRECLG EENLSVLKKG
     FENLKKHVEN IQKFGLSAVV AINHFPEDSE RELDCLLDMC SQIGVPAAVS EVWEKGSKGG
     LELAEKLLDI LENKGEDFRL LYDLELPIKE KIEIIAKEIY GADGVDYSPT ALNQIEKFEH
     MGYGKLPICM AKTQYSLSDD PAKIGRPRGF TINVREVRLS AGAGFIVPVT GDIMTMPGLP
     KKPAACKMDI DADGTIRGLF
//
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