ID A0A1G6RHG8_PEPNI Unreviewed; 554 AA.
AC A0A1G6RHG8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04489866_10113 {ECO:0000313|EMBL:SDD03366.1};
OS Peptococcus niger.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Peptococcus.
OX NCBI_TaxID=2741 {ECO:0000313|EMBL:SDD03366.1, ECO:0000313|Proteomes:UP000198995};
RN [1] {ECO:0000313|EMBL:SDD03366.1, ECO:0000313|Proteomes:UP000198995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20475 {ECO:0000313|EMBL:SDD03366.1,
RC ECO:0000313|Proteomes:UP000198995};
RA de Groot N.N.;
RL Submitted (OCT-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; FNAF01000001; SDD03366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6RHG8; -.
DR STRING; 2741.SAMN04489866_10113; -.
DR OrthoDB; 9761733at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000198995; 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:SDD03366.1};
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:UP000198995}.
FT BINDING 63..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ SEQUENCE 554 AA; 59051 MW; EE0CD9B1A614AD40 CRC64;
MKTDIEIANS VTPQPIEKIA EQLNISKEDL YLYGPYKAKL NLSLAENRPS KGKLILVTAI
NPTPAGEGKT TTTVGLGDAL AKAGHRTVIA LREPSLGPVF GIKGGATGGG YAQVIPMEDI
NLHFTGDMHA ITAANNLLAA AIDNHIHQGN ALGIDPRRII WKRCLDMNDR ALRKIVCSLG
GPTNGMPREE GFDITVASEV MAILCLAKDL EDLKTRLGRI VVAENFSGDY VLAKDLEVQG
AMAMLLKDAL KPNLVQTLEH TPAIIHGGPF ANIAHGCNSV TATKMALAFG DIAVTEAGFG
ADLGAEKFFD IKCRYAGLTP DAVVVVATVR ALKYNGGLPK SELEAENLPA LEKGLPNLLR
HLDNIQNVYG LPAVVAINRF PTDTEAEINL IRKACERQGV EVALSEVWAK GSAGGAELAK
AVLSLLQAPR DFRYAYQLEA PIEVKIRELV QKIYHGRDVT FSKTAQNAIA HLTAAGYAHL
PICMAKTQYS FSDDATQLGA PEGFTVTVQD LHVSAGAGFI VVLCGNILTM PGLPKKPAAN
QMDIAADGTI TGLF
//