FTHS_BACCQ
ID FTHS_BACCQ Reviewed; 562 AA.
AC B9IYP4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=BCQ_2085;
OS Bacillus cereus (strain Q1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=19060151; DOI=10.1128/jb.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-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:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR EMBL; CP000227; ACM12513.1; -; Genomic_DNA.
DR RefSeq; WP_012644371.1; NC_011969.1.
DR AlphaFoldDB; B9IYP4; -.
DR SMR; B9IYP4; -.
DR EnsemblBacteria; ACM12513; ACM12513; BCQ_2085.
DR KEGG; bcq:BCQ_2085; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000441; 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; 3.40.50.300; -; 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; SSF52540; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism.
FT CHAIN 1..562
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000185247"
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 562 AA; 60476 MW; AE56CAD4C8D76E35 CRC64;
MTTTTTVKSD IEIAQEASMK KIQEIAAELN ILEDELEPYG HYKGKLSLDI FKRLQNEKDG
KVVLVTAINP TPAGEGKSTV TVGLGQAFNK IGKKTVIALR EPSLGPTMGL KGGAAGGGFS
QVVPMEDINL HFTGDIHAIT TANNALAAFI DNHIQQGNTL GIDTRKIVWK RCVDLNDRAL
RNVVIGLGGP VQGVPREDGF DITVASEIMA VFCLATDIQD LKARLSRIVV AYNFANQPVT
VKDLGVEGAL TLLLKDALKP NLVQTLENTP AIIHGGPFAN IAHGCNSVIA TTMAAKLGDY
VITEAGFGAD LGAEKFLDIK ARAAGIKPEA VVIVATIRAL KMHGGVAKDQ LKEENVDALA
KGMENLQKHV ETIQSFGVPF VIAINKFITD TDAEVAYLQE WCNERGYAVS LTEVWEKGGQ
GGVDLAEKVL KEIEKGENNY APLYELELPL EEKIRTIAQK VYGAKDIEFA PKARKQLAQY
EGEGWSNLPI CMAKTQYSLS DDATKLGRPS DFIVTIRELK PSIGAGFIVA LTGTMLTMPG
LPKQPAALQM DVNEDGKAVG LF
