FTHS_HALMA
ID FTHS_HALMA Reviewed; 553 AA.
AC Q5V5Y2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 86.
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=pNG7380;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OG Plasmid pNG700.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV45070.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY596296; AAV45070.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5V5Y2; -.
DR SMR; Q5V5Y2; -.
DR EnsemblBacteria; AAV45070; AAV45070; pNG7380.
DR KEGG; hma:pNG7380; -.
DR PATRIC; fig|272569.17.peg.800; -.
DR HOGENOM; CLU_003601_3_3_2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001169; Plasmid pNG700.
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; Plasmid;
KW Reference proteome.
FT CHAIN 1..553
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199413"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 553 AA; 59251 MW; 6FDA27CFF8595A76 CRC64;
MEPIWELVEP WGLGLDDLQY FGEYTAKVKQ HAIERLREQA ENREQNLVLV TGMTPTPKGE
GKTVTTVGLG QTLNHVGEEA MIAIREPSLG PVFGVKGGAA GGGRSQVLPM EDINLHFTGD
LHALTSAHNL IAAMLDAKIS QGDDLNIDIN NVSWPRAIDM NDRALRETVV GLGGKTGGTP
REDSFILTAA SELMAVLCLA SDIGDLKERV SRIIVAYDED GDPVTVEDIE ATGPATMLLR
DAIKPNVVQT IEGTPALVHG GPFANIAHGT NSLVADKTAF GMGDYLVTEA GFGSDLGAEK
FMDVVCRKGD MTPNAVVLVA SVRALKYHGL NQWPVDYDEI GEAGVEAVEA GFSNLDKHAR
NLQKFGVPVV VSVNRFPDDT DEEVQAVLDH CREDLGVRAA ESNVFSDGSE GGVDLAENVI
EATEESNEED FRMLYDDDDS IKEKIHTVAT EIYGADDVKY TGGALDDIEQ MNDLDFDDYP
VVMSKTFHSL SDDASQKGAP EGWELEISEV YPSAGAGFLV ALTADALTMP GLPARPAAAD
MDIDGDGNIS GLF