FTHS_LAWIP
ID FTHS_LAWIP Reviewed; 591 AA.
AC Q1MPZ9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=LI0874;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; AM180252; CAJ54928.1; -; Genomic_DNA.
DR RefSeq; WP_011526957.1; NC_008011.1.
DR AlphaFoldDB; Q1MPZ9; -.
DR SMR; Q1MPZ9; -.
DR STRING; 363253.LI0874; -.
DR KEGG; lip:LI0874; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_7; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002430; 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..591
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293044"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 591 AA; 64251 MW; C08387A37F820458 CRC64;
MSLSPLNYAD WEIAQAAEKH MKTVYDLGKD LGLDHKEIFP YGHYMGKVDY KSVLSRLEQS
SDGKYIDVTA ITPTPLGEGK STTTIGLVQG LAKRGKRSSA AIRQPSGGPT MGVKGSAAGG
GLSQCIPLTQ YSLGFTGDIN AVMNAHNLSM VALTSRMQHE RNYSDEKLYA LSNMKRLDID
PTNIPMGWVM DFCCQSLRNI IIGIDGVSGK SDGYMMRSHF DIAVSSEVMA ILAIAKDLKD
FRQRISKIIV AYDKQGKAIT TADLEVDGAM TAWMVEAINP NLIQSIEGQP IFVHAGPFAN
IAIGQSSVIA DRLGLKLSEY HVTESGFGVD IGYEKFWNLK CHYSGLTPDA AVIVTTVRAL
KSHGGAPIPI PGRPLPKEYT EENVGYVEVG SANLIHHINT VKKSGVPPVV CINAFTTDTP
SEIAKIRQLC ELVGARVAVS KHWEYGGDGA LELADAVIDA CNEEKNFLPL YDWSLPLKER
IEKIAFEVYG AEGVEFSEEA IYKLNKLQAD NNSSDLGVCM VKTHLSLSDD PKQKGVPDHW
KLHVRDIMFF GGAGFVVPIA GSITLMPGTG SNPSFRRIDV DTDTGKVKGI F
