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Database: UniProt
Entry: A9QPK0_METI4
LinkDB: A9QPK0_METI4
Original site: A9QPK0_METI4 
ID   A9QPK0_METI4            Unreviewed;       562 AA.
AC   A9QPK0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=ftfL {ECO:0000313|EMBL:ABX56658.1};
GN   Synonyms=fhs {ECO:0000256|HAMAP-Rule:MF_01543}, mIS1
GN   {ECO:0000313|EMBL:ACD82431.1};
GN   OrderedLocusNames=Minf_0373 {ECO:0000313|EMBL:ACD82431.1};
OS   Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS   V4)).
OC   Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales;
OC   Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023).
OX   NCBI_TaxID=481448 {ECO:0000313|EMBL:ABX56658.1};
RN   [1] {ECO:0000313|EMBL:ABX56658.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=V4 {ECO:0000313|EMBL:ABX56658.1};
RX   PubMed=18004300; DOI=10.1038/nature06411;
RA   Dunfield P.F., Yuryev A., Senin P., Smirnova A.V., Stott M.B., Hou S.,
RA   Ly B., Saw J.H., Zhou Z., Ren Y., Wang J., Mountain B.W., Crowe M.A.,
RA   Weatherby T.M., Bodelier P.L.E., Liesack W., Feng L., Wang L., Alam M.;
RT   "Methane oxidation by an extremely acidophilic bacterium of the phylum
RT   Verrucomicrobia.";
RL   Nature 450:879-882(2007).
RN   [2] {ECO:0000313|EMBL:ACD82431.1, ECO:0000313|Proteomes:UP000009149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate V4 {ECO:0000313|Proteomes:UP000009149}, and V4
RC   {ECO:0000313|EMBL:ACD82431.1};
RX   PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA   Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA   Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA   Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA   Feng L., Wang L., Alam M.;
RT   "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT   V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT   Verrucomicrobia.";
RL   Biol. Direct 3:26-26(2008).
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|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; EU223916; ABX56658.1; -; Genomic_DNA.
DR   EMBL; CP000975; ACD82431.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9QPK0; -.
DR   STRING; 481448.Minf_0373; -.
DR   KEGG; min:Minf_0373; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_0; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000009149; 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; 3.30.1510.10; 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; IPR027417; P-loop_NTPase.
DR   Pfam; PF01268; FTHFS; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01543};
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         71..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   562 AA;  61082 MW;  8F55499A3F046708 CRC64;
     MKEKNLSSDL KIAREKKPLG IEEVAKKLSI PHDALERYGA FKAKISWEYL KELFCRPRRG
     KLVLVTATTP TPAGEGKTTT AIGLTDGLSR LGQKAALCLR EPSMGPVFGA KGAATGSGLA
     QLIPREEINL HFTGDFAAVA AAHNLLAALI DNHLYHGNDL GIDPRKISWG RVVDINDRAL
     RKILVGLESK KSFPRFSFFD IVAASEVMAI LCLAQSYKDL RQRIADICIG RGRDDKNIDA
     EELGAAGAMS VLLVHAFKPN LVQTLENNPA FVHGGPFGNI AHGCSSVVSL NAALRLADWV
     VTEAGFGSDL GGEKFVNIVC RQSGLKPDCA VIVTTVRALK FHGGMTLDCL NQRDLYSLEK
     GFPNLLRHIQ IVEEVLGIPA VVALNRFSAD SGEEIDWLGK RLGSLGYPFA VCNHWAQGGE
     GAVELARRVL ERSRQLNCKL NFTYADGDPL IKKIEKIALN VYKAGSIALH PHAQEEIRVI
     ERQGLDQLPV CMAKTQYSFS VDPRLRGAPE GHELFVRELR VAAGAKYILV LCGEINTMPG
     LPKVPASSSM DIDEEGKVIG TI
//
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