FTHS_CERS1
ID FTHS_CERS1 Reviewed; 557 AA.
AC A3PM52;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=Rsph17029_2316;
OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL Submitted (FEB-2007) 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; CP000577; ABN77418.1; -; Genomic_DNA.
DR RefSeq; WP_002720843.1; NC_009049.1.
DR AlphaFoldDB; A3PM52; -.
DR SMR; A3PM52; -.
DR EnsemblBacteria; ABN77418; ABN77418; Rsph17029_2316.
DR GeneID; 57470987; -.
DR KEGG; rsh:Rsph17029_2316; -.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
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..557
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300535"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 59619 MW; 70FA3F19090AF783 CRC64;
MAVQTDIEIA RAARKKPIQE IGAGLGIPAE ALIPYGHDKA KVGQGFIRGL EGRPDGKLIL
VTAINPTPAG EGKTTTTVGL GDGLNRIGKK AVICIREASL GPNFGMKGGA AGGGRAQVVP
MEDMNLHFTG DFHAITAAHN LLAAMIDNHI YWGNALELDA RRITWRRVMD MNDRALRDTV
VNLGGVANGF PRQTGFDITV ASEVMAILCL ADDLEDLERR LGRIVVGYRR DKSPVYCRDL
KAAGAMAVLL KDAMQPNLVQ TIENNPAFVH GGPFANIAHG CNSVIATRTA LKLADYVVTE
AGFGADLGAE KFFDIKCRLA GLKPSAAVVV ATVRALKMNG GVAREDLGRE DVAALRRGCA
NLGRHIANVK GFGVPVVVAI NHFTTDTEAE IEAVRAYAAG QGAEAFLCRH WAEGSAGIED
LAQKVVELAE TPSMFAPLYP DDMPLFEKME TVARRIYHAH DVIADHVIRD QLRTWEEAGY
GALPVCMAKT QYSFTTDAAI RGAPEGHSIP IREVRLAAGA GFVVAICGEI RTMPGLPSQP
AAELIHLDEE GRIEGLF