ID A8AXI7_STRGC Unreviewed; 556 AA.
AC A8AXI7;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
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-1 {ECO:0000313|EMBL:ABV10337.1};
GN Synonyms=fhs {ECO:0000256|HAMAP-Rule:MF_01543};
GN OrderedLocusNames=SGO_1210 {ECO:0000313|EMBL:ABV10337.1};
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV10337.1, ECO:0000313|Proteomes:UP000001131};
RN [1] {ECO:0000313|EMBL:ABV10337.1, ECO:0000313|Proteomes:UP000001131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC {ECO:0000313|Proteomes:UP000001131};
RX PubMed=17720781; DOI=10.1128/JB.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV10337.1; -; Genomic_DNA.
DR RefSeq; WP_012000611.1; NC_009785.1.
DR AlphaFoldDB; A8AXI7; -.
DR STRING; 467705.SGO_1210; -.
DR KEGG; sgo:SGO_1210; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001131; 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:ABV10337.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01543};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_01543}; Reference proteome {ECO:0000313|Proteomes:UP000001131}.
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 59793 MW; 218496AD367026AE CRC64;
MKTDIEIAQS IELQPIVDVV KKIGIDYDDL ELYGKYKAKL SFDKISEVRK NPVGKLILVT
AINPTPAGEG KSTITIGLAD ALNKIGKKTM IAIREPSLGP VMGIKGGAAG GGYAQVLPME
DINLHFTGDM HAITTANNAL SALIDNHLHQ GNDLGIDQRR IIWKRVVDLN DRALRHVTVG
LGSPVNGIPR EDGFDITVAS EIMAILCLAT DIEDLKNRLA NIVIGYRYDR SPVYVRDLEV
EGALALVLKD AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATSTALR LADYTVTEAG
FGADLGAEKF LDIKTPNLPT SPDAVVIVAT LRALKMNGGV AKDALTEENV EAVRAGFANL
KRHVENIRKF GIPAVVAINE FVSDTEAEIA TLKELCAEIG VPVELASVWA DGAEGGVALA
EAAVKTINEE PAHYTRLYDN ELSIEEKIEK IVTEIYRGSK VNFEKKAQTQ IREIIKNGWD
KLPICMAKTQ YSFSDNPAAL GAPENFEITI RELVPKLGAG FIVALTGDVM TMPGLPKRPA
ALNMDVASDG TAIGLF
//
