ID C5NYX8_9BACL Unreviewed; 551 AA.
AC C5NYX8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 57.
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 ECO:0000313|EMBL:EER67765.1};
GN ORFNames=GEMHA0001_0668 {ECO:0000313|EMBL:EER67765.1};
OS Gemella haemolysans ATCC 10379.
OC Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX NCBI_TaxID=546270 {ECO:0000313|EMBL:EER67765.1, ECO:0000313|Proteomes:UP000006004};
RN [1] {ECO:0000313|EMBL:EER67765.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67765.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EER67765.1, ECO:0000313|Proteomes:UP000006004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10379 {ECO:0000313|EMBL:EER67765.1,
RC ECO:0000313|Proteomes:UP000006004};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (JUN-2009) 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|HAMAP-Rule:MF_01543}.
CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC {ECO:0000256|HAMAP-Rule:MF_01543}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EER67765.1}.
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DR EMBL; ACDZ02000014; EER67765.1; -; Genomic_DNA.
DR RefSeq; WP_003145133.1; NZ_ACDZ02000014.1.
DR AlphaFoldDB; C5NYX8; -.
DR GeneID; 78010232; -.
DR eggNOG; COG2759; Bacteria.
DR OrthoDB; 9761733at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006004; Unassembled WGS sequence.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF01268; FTHFS; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01543, ECO:0000313|EMBL:EER67765.1};
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 COILED 337..364
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ SEQUENCE 551 AA; 59780 MW; 30147B3E80104166 CRC64;
MKSDFQISNE CEKKHIAEVA GKLGIKEEDL ILYGNHKAKI QTKNIKKDIN DDAKLVLVTS
INPTSSGEGK STVTIGLSDG LNRIGKKSCV ALREPSLGPV LGRKGGAAGG GYAQVVPMED
INLHFTGDMH AITTAHNAIA VLVNNHVFQG NELEIDKIVF NRVMDMNARD LRHIKVNAGT
DLERLDGFDI TVASEVMAIL CLSEGIADLK EKLSNILVAY NKKGEPVYLK DLKIEGVITS
LLKDAIKPNI VQTLENNPAI IHGGPFANIA HGCNSILATK TALKFADYVI TEAGFGADLG
AEKFLNIKCR KAGLKPKAAV VVATVKALKL HGDIEEKDLK EENLEALAKG VQNLEKHIEN
LRKFNLPIVV ALNVFVTDTE KELAFLENWA KEQGVEFSRT EVWEKGGLGG VDLAEKVVKA
VEGNDKELQL LYKDEASITE KIETVCREIY GADGVNFSDE AKAEIERIES LGFKHLPVCM
AKTPASLTDN AKIKGRPTGF NITINDVKLR SGAGFVVAYA NKVLTMPGLP KVPSALNIDI
DEETETIVGI F
//
