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Database: UniProt
Entry: A0A1N6RCT4_9SPIO
LinkDB: A0A1N6RCT4_9SPIO
Original site: A0A1N6RCT4_9SPIO 
ID   A0A1N6RCT4_9SPIO        Unreviewed;       580 AA.
AC   A0A1N6RCT4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=SAMN05920897_10655 {ECO:0000313|EMBL:SIQ26609.1};
OS   Alkalispirochaeta americana.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Alkalispirochaeta.
OX   NCBI_TaxID=159291 {ECO:0000313|EMBL:SIQ26609.1, ECO:0000313|Proteomes:UP000186400};
RN   [1] {ECO:0000313|EMBL:SIQ26609.1, ECO:0000313|Proteomes:UP000186400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASpG1 {ECO:0000313|EMBL:SIQ26609.1,
RC   ECO:0000313|Proteomes:UP000186400};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; FTMS01000006; SIQ26609.1; -; Genomic_DNA.
DR   RefSeq; WP_076488426.1; NZ_FTMS01000006.1.
DR   AlphaFoldDB; A0A1N6RCT4; -.
DR   STRING; 159291.SAMN05920897_10655; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000186400; 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:SIQ26609.1};
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:UP000186400}.
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   580 AA;  61756 MW;  E88DEB6E45B87B17 CRC64;
     MRLSDLEIAQ AAQVEPIETI AARLGLASGE WLPWGRNIAK VDPAVARGER HPDSRYIDVT
     AITPTPLGEG KTTTTVGLTQ GLGAIGRKGM CAIRQPSQGP TFGIKGGAAG GGYSQVLPME
     EFNLHLTGDI HAITAAHNLI AAAIDNQMYH ESRWSDAFFQ KRGIEKVHID PYEISWNRVV
     DLNDRSLRSV VTGLGALADG PLRQGGFDIT VASELMAVLA LARDLRDLRE RIGRIVVALD
     RGGAPVTTED LGVAGAATVL LRDALWPNLL QTLEGQPAFV HAGPFANIAH GNSSVMADRI
     ALTQGGFLVT ESGFGADIGM EKFFDIKCRV SGLMPDAVVL VATIRALKMH GGGPAVTPGR
     PLPQEYCQEN LELLRSGLDN LRAHIRIAGL FGVPLVVAVN AFDTDTEGEL ALVRDAALQA
     GAADAVVTHH HARGGEGALA LAEAVARAAD APRTTSPSPL YDLSLPLEEK LRTVATRVYG
     ARDIELSPLA RRQIARYEEE GYGTMPVCIA KTHLSLSHDP ALKNAPENFI FPVRELRPSA
     GAGFVYALAG DIRTMPGLPS VPAFRGIDID VETGRVQGLF
//
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