FTHS_ELUMP
ID FTHS_ELUMP Reviewed; 556 AA.
AC B2KDK9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Emin_1052;
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191;
RX PubMed=19270133; DOI=10.1128/aem.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(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; CP001055; ACC98605.1; -; Genomic_DNA.
DR RefSeq; WP_012415220.1; NC_010644.1.
DR AlphaFoldDB; B2KDK9; -.
DR SMR; B2KDK9; -.
DR STRING; 445932.Emin_1052; -.
DR EnsemblBacteria; ACC98605; ACC98605; Emin_1052.
DR KEGG; emi:Emin_1052; -.
DR HOGENOM; CLU_003601_3_3_0; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001029; 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;
KW Reference proteome.
FT CHAIN 1..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000146682"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 59643 MW; 1F7C40552C960A33 CRC64;
MLSDIEIAQR AKVWPIAKVA VKLGIKKSQI ELYGHYKAKL SFDCIKKLQK KPDGNLILVT
AISPTAAGEG KSTTTVGLAQ ALAKIGKKAI VALREPSLGP CMGIKGGAAG GGYSQVVPME
DINLHFTGDM HAITAANNLL SAIIDNHIHQ GNELGIDERR IVWHRVVDIN DRALRNIVVA
LGGKGNGFPR EDSFDITVAS EVMAILCLSE SLADLKKRLS KVIVGYNFAD KPVTAGMLKA
EGAMAALLKD AIKPNLVQTL ENVPAIIHGG PFANIAHGCN SVIATKTALK LADYIVTEAG
FGADLGAEKF FNIKCRYAGL TPKVAIIVAT VRALKMHGGV SKDKLTHLDK QAVIRGLVNL
DKHIENVKKF GVPPVVAINI FSGDSKEEIA AVKAHCKKIG VPVELSDVFA KGGEGGIQLA
KKVVDIISKN KSKFRFTYES EDSLEEKTKK IVKNIYGAKD VFFDKKALDS IKKYEAMGFG
NIPVCMAKTQ YSFSDNPKLY GRPEGFTIEV REARISAGAG FVVMLTGNIM TMPGLPKFPA
AEKIDISSEG VIKGLS
