ID A0A1W6BHW1_9PROT Unreviewed; 559 AA.
AC A0A1W6BHW1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000256|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000256|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000256|HAMAP-Rule:MF_01543};
DE Short=FHS {ECO:0000256|HAMAP-Rule:MF_01543};
DE Short=FTHFS {ECO:0000256|HAMAP-Rule:MF_01543};
GN Name=fhs {ECO:0000256|HAMAP-Rule:MF_01543};
GN ORFNames=B8063_05460 {ECO:0000313|EMBL:ARJ49462.1};
OS Candidatus Pelagibacter sp. RS40.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1977865 {ECO:0000313|EMBL:ARJ49462.1, ECO:0000313|Proteomes:UP000192922};
RN [1] {ECO:0000313|EMBL:ARJ49462.1, ECO:0000313|Proteomes:UP000192922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS40 {ECO:0000313|EMBL:ARJ49462.1,
RC ECO:0000313|Proteomes:UP000192922};
RA Jimenez-Infante F., Ngugi D.K., Stingl U.;
RT "Genomic Characterization of Two Novel SAR11 Isolates From the Red Sea,
RT Including the First Strain of the SAR11 Ib clade.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216;
CC EC=6.3.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01543};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|HAMAP-Rule:MF_01543}.
CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC {ECO:0000256|HAMAP-Rule:MF_01543}.
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DR EMBL; CP020778; ARJ49462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6BHW1; -.
DR STRING; 1977865.B8063_05460; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000192922; 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1.
DR Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01543, ECO:0000313|EMBL:ARJ49462.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_01543}.
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ SEQUENCE 559 AA; 61200 MW; F894795513E1015B CRC64;
MPKTDIQIAR EAKMKPINEI LANINVPDEP NAFSPMGRHI AKINLEYLDQ LKEKKNGKLI
LVTAITPTPA GEGKTTTSVG LSDGLNKIGK KSIVCLREPS LGPSFGMKGG AAGGGYAQVV
PMEQINLHFT GDFHAITSAH NLLSALIDNH IYWGNKLNID VRRVVWKRVM DMNDRSLRSI
VVDLGGIANG YPRQDGFDIT VASEIMAIFC LANNLKDLEK RIGNITIAYT REKKPIFAKD
LNAQGPMTVL LKEAIRPNVT QTLENNPAII HGGPFANIAH GCNSVIATKA GLKLSDYVVT
EAGFGADLGA EKFLDIKCRK SEIKPDCVVI VATIRALKMH GGVPKEDLKN ENVDALKKGL
VNLERHINNT RKFGLPVTIA VNHFITDTDK EMNTLLDFCK TQGVKASKCT HWSNGSEGTT
ELAKNVVEIC EETKNTFQYL YEDSLPLFKK IEKIAQEIYH ASEVVADSKV RQQLKDFEEK
GYGNLPVCIA KTQYSFSTDP NLKGAPTGHV LPVREVRLSS GAEFVVVVCG EIMTMPGLPR
VPAADSIKLN DEGEIEGLF
//
