FTHS_ACHLI
ID FTHS_ACHLI Reviewed; 527 AA.
AC A9NE95;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=ACL_0032;
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Acholeplasma.
OX NCBI_TaxID=441768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A;
RX PubMed=21784942; DOI=10.1128/jb.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
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; CP000896; ABX80675.1; -; Genomic_DNA.
DR RefSeq; WP_012242006.1; NC_010163.1.
DR AlphaFoldDB; A9NE95; -.
DR SMR; A9NE95; -.
DR STRING; 441768.ACL_0032; -.
DR EnsemblBacteria; ABX80675; ABX80675; ACL_0032.
DR GeneID; 66294162; -.
DR KEGG; acl:ACL_0032; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_14; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000008558; 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 Gene3D; 3.40.50.300; -; 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; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..527
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000333311"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 527 AA; 58201 MW; 7C37DFF8C7435489 CRC64;
MNTYNYLIDE LHILDDEIIS YGKDKFKIEL SLQERLKDKA PGKLILVTSI NPTSSGEGKT
TLSIGLAQGF KKNGKDVMLA LREPSMGPVF GMKGGATGGG VSILEPSLDI DLHFNGDIHA
LTSANNLLSA IIDNHMYFGN ELNIKDVYWQ RALDVNDRSL REVKTKARDD KFTITAASEM
MAILALARDF KDLKERLNNI LIGTDKDGKD LFVSDLKCAD SLALLLKDAI KPNLVFAKEM
VPALVHAGPF ANIAHGCNSV IATNTALKLA DYVITEAGFG ADLGMEKFLH IKQPHLYTKA
SVVVVVATIK ALKLHGGVTE SNLDEPNIEA LSKGLENIEK HLENIKLFGL NSVVALNKFD
TDSEEELQFL KNWARINHLN YGISEGYSKG GEGTKDLAKL VEKVAYEPSK FKRIYSNEEN
HEYKIRKIAE NIYGAKDVIF SQQAKKKLNQ YKHLEIPICI AKTPLSLSGD PKLKGRPRDF
VLEISDIKVS LGANLLVVLT KGINTMPGLN NRPRALDFKL DDKGELI
