ID E0NDL2_PEDAC Unreviewed; 555 AA.
AC E0NDL2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
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:EFL96333.1};
GN ORFNames=HMPREF0623_0384 {ECO:0000313|EMBL:EFL96333.1};
OS Pediococcus acidilactici DSM 20284.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL96333.1, ECO:0000313|Proteomes:UP000004470};
RN [1] {ECO:0000313|EMBL:EFL96333.1, ECO:0000313|Proteomes:UP000004470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL96333.1,
RC ECO:0000313|Proteomes:UP000004470};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) 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}.
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:EFL96333.1}.
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DR EMBL; AEEG01000002; EFL96333.1; -; Genomic_DNA.
DR RefSeq; WP_004165846.1; NZ_GL397067.1.
DR AlphaFoldDB; E0NDL2; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000004470; 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; 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:EFL96333.1};
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:UP000004470}.
FT BINDING 63..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ SEQUENCE 555 AA; 59658 MW; FB596E295DB74700 CRC64;
MNDIEISQNA EMLPIQEIAQ QAGFNEKTVE PYGRYKAKID IFAEDEEAAQ LGKLVLVTSI
NPTPAGEGKS TVTVGLGDAL NEMTGSAMVA LREPSQGPVM GMKGGATGGG YSQVVPMDEI
NLHFTGDMHA LTAANNTLAA LIDNHIQQGN QLNIDPRTIV WRRCLDINDR ALRNIVIGMG
GRFSGVPRED HFDITVASEL MAILCLAESL TDLKKRINRI LIAKNYAGEP IFVRDLKVGG
AITALLKDAL KPNLVQTLGH TPALIHGGPF ANIAHGCNSV LATKTALKHA DYTITEAGFG
ADLGAEKFLD IKTPVLGKEP DAIVIVATVR ALKYNGGAKL ADLQNEDLVA LEKGFVNLQR
HIKNMQRYQV PVVISINHFT SDTDQEIAEL KQLVEQTGVQ AVVTDAWAKG GAGCKELAQA
VITATDTNSD VTMQPLYDVA APIQDKVKAI VQKMYGGAEV QYSATALKKI KECEQNGWDK
LPICMAKTQY SFTDDPKQLG APTGFTMHVN DINIRLGAGF LVVLTGKVLT MPGLPKQPAA
LNIDVNDKGE ITGLF
//
