FTHS_GRABC
ID FTHS_GRABC Reviewed; 572 AA.
AC Q0BW57;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN OrderedLocusNames=GbCGDNIH1_0047;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(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; CP000394; ABI60945.1; -; Genomic_DNA.
DR RefSeq; WP_011630755.1; NC_008343.2.
DR AlphaFoldDB; Q0BW57; -.
DR SMR; Q0BW57; -.
DR STRING; 391165.GbCGDNIH1_0047; -.
DR EnsemblBacteria; ABI60945; ABI60945; GbCGDNIH1_0047.
DR GeneID; 56914445; -.
DR KEGG; gbe:GbCGDNIH1_0047; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001963; 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..572
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293036"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 572 AA; 60606 MW; 6D804024DA30ADD2 CRC64;
MSTEANKPRG NQHQEAKSDA EIAQAAFMRP IVDVAAEKLG IAAEHLAPYG HYKAKIDLNY
LSSLDSRPDG KLVLVTAISP TPAGEGKTTT TVGLTDALNH IGKKAVACLR EPSLGPCFGV
KGGAAGGGYA QVVPMEDINL HFTGDFHAIG AANNLLAALI DNHVYWGNEL GIDPRRIGWR
RAVDMNDRAL RSIVSSLGGV SNGYPREDGF DITVASEVMA IFCLATDLDD LQRRLGNIIV
GHTKDRKPIR ASELSAAGSM AVLLKDAIAP NLVQTLEHNP AFIHGGPFAN IAHGCNSVIA
TRAALKLSDY VVTEAGFGAD LGAEKFFDIK CRKAGLSPSA VVIVATVRAL KMHGGVAKDA
LKTENVEAVQ KGFANLERHI QNVRKFGVPV VVGVNKFSAD TDAEFQMLHD LCAKMGVPCV
SSDHWANGGA GAADLAHEVV KLVEGGSADF KPLYPEDMPL WDKLRTIATE IYGASDITAD
AAVRKRFDEL QKEGFGHLPI CVAKTQYSFS TDANLRGAPS GHVIPVRDLR LSAGAEFVVA
ICGDIMTMPG LPKVPAANAI RLASNGTIAG LF
