FTHS_RHIEC
ID FTHS_RHIEC Reviewed; 559 AA.
AC Q2K5P2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=RHE_CH03078;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC91844.1; -; Genomic_DNA.
DR RefSeq; WP_011426314.1; NC_007761.1.
DR AlphaFoldDB; Q2K5P2; -.
DR SMR; Q2K5P2; -.
DR STRING; 347834.RHE_CH03078; -.
DR EnsemblBacteria; ABC91844; ABC91844; RHE_CH03078.
DR KEGG; ret:RHE_CH03078; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001936; 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..559
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293052"
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; 59740 MW; 77EE4A7AB92E53A6 CRC64;
MPSIKSDIEI ARAATKRPIF EIGAKLGIAA EQLVPYGHDK AKVSAEFIAA QAGKKDGKLI
LVTAINPTPA GEGKTTTTVG LGDGLNRIGK KAIVCIREAS LGPCFGVKGG AAGGGYAQVV
PMEDINLHFT GDFHAITSAH NLLAAIIDNH IYWGNEENID IRRITWRRVM DMNDRALRSM
ISSLGGVANG FPRQGGFDIT VASEVMAILC LATDLKDLER RLGDIIIGYR FDKTPVHARD
LKADGAMAVL LKDAMQPNLV QTLESNPAFV HGGPFANIAH GCNSVTATKT ALKLGEYVVT
EAGFGADLGA EKFFDIKCRK AGLRPDAAVI VATVRALKMN GGVKKEDLGT EDVAALKKGC
ANLGRHVANV RRFGVPVVVA INHFVSDTDA EIAAVKEFVS RLGAEAILCQ HWAKGSAGIE
ELAHKVVELA ESGQAKFQPL YGDDISLFEK IEIIASKIYH AGEVTADKAV RDQLQSWEEQ
GYGKLPVCMA KTQYSFSTDP NLRGAPEGHI VSVREVRLSA GAGFVVAITG EIMTMPGLPK
SPSAERIFLN DQGYIEGLF
