FTHS_RHILO
ID FTHS_RHILO Reviewed; 559 AA.
AC Q98HQ4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=mlr2763;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB49812.1; -; Genomic_DNA.
DR RefSeq; WP_010911161.1; NC_002678.2.
DR AlphaFoldDB; Q98HQ4; -.
DR SMR; Q98HQ4; -.
DR STRING; 266835.14023205; -.
DR EnsemblBacteria; BAB49812; BAB49812; BAB49812.
DR GeneID; 66682431; -.
DR KEGG; mlo:mlr2763; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000552; 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..559
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199371"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 559 AA; 59971 MW; 28FD5270D2672978 CRC64;
MAEVKSDIEI ARAAKKKQIQ EIGQKIGIPT EHLLPYGHDK AKISAEFIKS VKGNKDGKLI
LVTAINPTPA GEGKTTTTVG LGDGLNRIGK KAIVCIREAS LGPNFGVKGG AAGGGYAQVV
PMEDMNLHFT GDFHAITTAH NLLSALIDNH IYWGNELGID TRRVVWRRVM DMNDRALREM
ICSLGGVANG FPREGGFDIT VASEVMAILC LSTDLKDLEK RLGDIIVAYR RDKSPVYARD
LKADGAMAVL LKDAMQPNLV QTLENNPAFV HGGPFANIAH GCNSVVATTT ALKLADYVVT
EAGFGADLGA EKFFDIKCRK AGLKPAAAVI VATVRAMKMN GGVKKEDLGK ENIEAVKKGC
ANLGRHIENI RQFGVPAVVA INHFYSDTDA EIQAMKDYVA SMGEEAVLCK HWAKGSAGIE
ELANKVVALA ESGASQFAPL YPDAMPLFEK INTIVQRIYR GSEAIADKSV RDQLHAWEQA
GYGNLPVCMA KTQYSFSTDP NLRGAPTGHT VPVREVRLSA GAGFVVIICG EVMTMPGLPK
APSSEKIFLN EAGQIEGLF