FTHS_ROSDO
ID FTHS_ROSDO Reviewed; 558 AA.
AC Q160C2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=RD1_4235;
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG33671.1; -; Genomic_DNA.
DR RefSeq; WP_011570281.1; NZ_FOOO01000006.1.
DR AlphaFoldDB; Q160C2; -.
DR SMR; Q160C2; -.
DR STRING; 375451.RD1_4235; -.
DR EnsemblBacteria; ABG33671; ABG33671; RD1_4235.
DR KEGG; rde:RD1_4235; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000007029; 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..558
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300536"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 558 AA; 60126 MW; 3706CFA79DC30643 CRC64;
MAYKSDIEIA REAKKRPIQE IGEKIGIGSD DLLPYGHDKA KVSQSFINSV QDKPNGRLVL
VTAINPTPAG EGKTTTTVGL GDGLNHIGKN AMICIREASL GPNFGMKGGA AGGGYAQVVP
MEDMNLHFTG DFHAITSAHS LLSAMIDNHI YWGNEAEIDV RRVQWRRVVD MNDRALRQIT
ASLGGVANGF PREAGFDITV ASEVMAILCL AKDLKDLEKR LGDMIVAYRR DRSPVFCRDI
KAQGAMTVLL KDAMQPNLVQ TLENNPAFVH GGPFANIAHG CNSVIATTTA LKLADYVVTE
AGFGADLGAE KFMNIKCRKA GIAPSVVVCV ATVRAMKMNG GVAKADLGAE NVDAVKKGCP
NLGRHIENLK SFGVPVIVAI NHFVTDTDAE VEAIKSYVSE HGAEAVLSRH WELGSEGSAD
LARKVVEVAE KDSANFAPIY PDDMPLAEKV QTIAKRIYRA DEALMDKKVR DQLKLWEEQG
YGHLPVCMAK TQYSFSTDPN LRGAPTGHSV PVREVRLSAG AGFVVVVCGE IMTMPGLPRV
PSAENIHLNE DGQIEGLF