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Database: UniProt
Entry: A0A221MD48_9BACI
LinkDB: A0A221MD48_9BACI
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ID   A0A221MD48_9BACI        Unreviewed;       556 AA.
AC   A0A221MD48;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-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=CFK40_11300 {ECO:0000313|EMBL:ASN05554.1};
OS   Virgibacillus necropolis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN05554.1, ECO:0000313|Proteomes:UP000204391};
RN   [1] {ECO:0000313|EMBL:ASN05554.1, ECO:0000313|Proteomes:UP000204391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN05554.1,
RC   ECO:0000313|Proteomes:UP000204391};
RX   PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA   Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA   Rodriguez-Diaz M., Swings J., De Vos P.;
RT   "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT   Virgibacillus picturae sp. nov., three novel species isolated from
RT   deteriorated mural paintings, transfer of the species of the genus
RT   salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT   Virgibacillus salexigens comb. nov., and emended description of the genus
RT   Virgibacillus.";
RL   Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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; CP022437; ASN05554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221MD48; -.
DR   KEGG; vne:CFK40_11300; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000204391; 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; 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:ASN05554.1};
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:UP000204391}.
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;  60479 MW;  2FC091E708462BE7 CRC64;
     MKTDIEIAQE AKLKSIGDIA KDLHLTENDW EPYGHTKAKL SDNLLKKLQD KPNGKVILVT
     SINPTPAGEG KSTVTVGLGQ ALNKLNKKAI IALREPSLGP VMGMKGGAAG GGYSQVLPME
     DINLHFTGDL HAITSANNAL SAIIDNHIHR GNELNIDPRR VEWKRVMDMN DRVLRQIVVG
     LGGPLRGIPR EDGFTITVAS EIMAILCLST GLEDLKKRIA RIVIGYTYEE EPVTVKDLKI
     EGALTLLLKD AIKPNLVQTT ENTPAIIHGG PFANIAHGCN SIMATKTAAK LGEYVVTEAG
     FGADLGAEKF LDIKSRAGEI DTAAVVIVAT VRALKMHGGV DKNNLKEENV EALKNGMSNL
     KKHIETVEQF GLPYVIAINK FPTDSEAETD FIHHWCESHG AEVALTDVWA RGGEGGIDLA
     KKVMAKADSD DRNFNYTYEI NETLETKIRM IAQKVYGADN IELSQKAKKQ LMFYEKQGWG
     KLPICMAKTQ YSLSDDPTLL GRPEGFTVSI REVQASIGAG FIVVLTGEMM TMPGLPKKPA
     AYNMDVTEDG KIVGLF
//
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