ID A0A160IL92_9BACI Unreviewed; 562 AA.
AC A0A160IL92;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ABE65_009470 {ECO:0000313|EMBL:ANC77018.1};
OS Fictibacillus phosphorivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC77018.1, ECO:0000313|Proteomes:UP000076623};
RN [1] {ECO:0000313|EMBL:ANC77018.1, ECO:0000313|Proteomes:UP000076623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-29 {ECO:0000313|EMBL:ANC77018.1,
RC ECO:0000313|Proteomes:UP000076623};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT toxic to nematodes.";
RL Submitted (APR-2016) 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; CP015378; ANC77018.1; -; Genomic_DNA.
DR RefSeq; WP_066394024.1; NZ_CP015378.1.
DR AlphaFoldDB; A0A160IL92; -.
DR STRING; 1221500.ABE65_009470; -.
DR KEGG; fpn:ABE65_009470; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000076623; 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:ANC77018.1};
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 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ SEQUENCE 562 AA; 60801 MW; AE99B61B6DD489AB CRC64;
MLEKVTFKSD IEIAQSAKML RIEEIVGQLG IEEDDWEPYG RYKGKLSLDL FQKLQNVEDG
KVVLVTAISP TPAGEGKSTV TVGLGQALNR VGKKTIIALR EPSLGPSMGI KGGAAGGGYS
QVMPMEDINL HFTGDLHAIT TANNALAALI DNHIHQGNEL NIDPRRIVWK RALDMNDRAL
RKIVIGLGGP IQGVPREDGF DITVASEVMA IFCLANDLED LKVRLSKMVV AFDYDNQPIT
AGHLNAQGAL TLLLKDAIRP NIVQTLENTP ALVHGGPFAN IAHGCNSVIA TKLASKLGEM
VVTEAGFGAD LGAEKFLDIK ARYAGINPSA VVIVATVRAL KMHGGLAKEY LKNPDLEALQ
KGMPNLEKHL ETLKEFGVPV VVAINKFVTD TDEEVAFIKE WCNSKGVAAE EADVWAKGGQ
GGEALANRVL ETIESEENNY KPLYELNVSL QEKIETICKK VYGAGEVQFS PKAVKQMKQF
TDFGWDQLPI CMAKTQYSFS DDPKKLGRPK NFTITIRELK PSIGAGFIVA LTGDVMTMPG
LPKVPAANNM DVSEDGKAVG LF
//
