FTHS_SACEN
ID FTHS_SACEN Reviewed; 565 AA.
AC A4FL80;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-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}; OrderedLocusNames=SACE_5619;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(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; AM420293; CAM04805.1; -; Genomic_DNA.
DR RefSeq; WP_009944604.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FL80; -.
DR SMR; A4FL80; -.
DR STRING; 405948.SACE_5619; -.
DR EnsemblBacteria; CAM04805; CAM04805; SACE_5619.
DR KEGG; sen:SACE_5619; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_11; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006728; 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..565
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293057"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 565 AA; 59922 MW; 8C202C45707AE1E3 CRC64;
MTVPSDLDIS RATALRPLED IAAQLGLGPH LLEPYGHNVA KISLDAIEEL SDRPQARYVV
VSAITPTPLG EGKTTTTVGL GQALRHLGKV SAVAVRQPSM GPTFGIKGGA AGGGYSQVVP
MEALNLHLTG DMHAVTAAHN LLSAMLDNHL HKGNRLGVDP HRITWRRVLD VNDRDLRNIV
TGMGGRADGT PRQTGFDITA ASEVMAVLAL STSLRDMRRR LGRIVVGYTR DGSPVTAEDL
RAAGAMTAIM REAIKPNLMQ TTENTPVLVH AGPFGNIAHG NSSVVADRIA GRCADYLVTE
AGFGADMGAE RFFNIKCRTS GMRPDAAVLV ATVRALKAHS GRYKVVAGRP LPPEMLAENP
DDVLAGAENL RKQIDNIRLH GVSPVVAVNA FPTDHGSEHD AIRRVAEEEG ARVAVSNHYS
EGGKGALELA EVVVEAAEEP NRFRLLYPDS ADLRTKIETI ATRVYGADGV SYQPAAARAL
ADYEAIGFGS LPVCIAKTHL SLSSDPSLLG APTGWTLPVR EVRASIGAGF IYAICGEMRT
MPGLGSHPAA ERIDIDEHGQ IVGLS