FTHS_BACP2
ID FTHS_BACP2 Reviewed; 560 AA.
AC A8FEC9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=BPUM_1926;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-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:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR EMBL; CP000813; ABV62596.1; -; Genomic_DNA.
DR RefSeq; WP_012010314.1; NZ_VEIS01000001.1.
DR AlphaFoldDB; A8FEC9; -.
DR SMR; A8FEC9; -.
DR STRING; 315750.BPUM_1926; -.
DR EnsemblBacteria; ABV62596; ABV62596; BPUM_1926.
DR KEGG; bpu:BPUM_1926; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001355; 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; 3.40.50.300; -; 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; SSF52540; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..560
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000318564"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 560 AA; 60467 MW; 06EBAA5FB9E818FB CRC64;
MITKHLSDID IAQQAKLRPI QDIAAKLQLH DEELECYGFT KAKISLTIFD RLKEQKEGHV
ILVTSINPTP AGEGKSTVTV GLGQAFEKIG KKAIIAMREP SLGPTMGIKG GAAGGGYSQV
LPMEEINLHF TGDFHAITSA HNALSAFIDN HIHHGNELDI DARRIVWKRV LDLNDRALRQ
VVVGLGGQVN GYPREDGFDI TVASEMMAIL CLAEDLTDLK KRLSSIVVAY NRDGEPVTVG
ALGYEGVLTL LLKDALKPNL VQTIEGTPAL VHGGPFANIA HGCNSLIATK MAAKLADYVV
TEAGFGADLG AEKFLNIKTR AGDFKPGAVV IVATVRALKM HGGMKKTELK EENTQAVLKG
IHNLEKHIET VQAFGLPYIV AVNRFITDTK EEIQAIEDWC LAHDHPVKAV NVWEEGGEGG
TALAEELTTL IEKKKNSFSY LYEEDDSIEE KLSKVAKVVY GADGVTLTSK ARKQLAAIEE
NSWGHLPVCM AKTQYSLSDD PALIGRPKGF TITIRELKPS VGAGFIVALT GSILTMPGLP
KKPAALEMDL LEDGSVTGLF