FTHS_NOCSJ
ID FTHS_NOCSJ Reviewed; 559 AA.
AC A1SQH3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Noca_4561;
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000509; ABL84058.1; -; Genomic_DNA.
DR RefSeq; WP_011757986.1; NC_008699.1.
DR AlphaFoldDB; A1SQH3; -.
DR SMR; A1SQH3; -.
DR STRING; 196162.Noca_4561; -.
DR EnsemblBacteria; ABL84058; ABL84058; Noca_4561.
DR KEGG; nca:Noca_4561; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_11; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000640; 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..559
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000293049"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 559 AA; 58921 MW; 6CCE6AECED3646C3 CRC64;
MLSDIEIAGA ATLRPITEVA TESLGIGAEH LVPYGHYKAK VGITYLNSLA DRPLGRLILV
TALSPTPPGE GKTTTSVGLT DALHGLGKRA IACLREPSMG PVFGLKGGAA GGGYSQVVPM
TDINLHFTGD FAAIAAANNL LAALIDNHVH HGNELDIDVR SVTWKRVLDT NDRALREVVV
GLGGPPNGFP RQDGFDIVVA SELMAIFCLT ESWADLKRRI GDIVIGYSRA GAPVTARDLG
ADGAMAVLLR DAIAPNLVQT LEGAPALVHG GPFANIAHGC SSVMATRAGL RLADYVVTEA
GFGADLGAEK FIDIKCRMSG MRPDVAVVVA TVRALKYHGG VALADLDRED LGAVEAGMDN
LRRHLDNLRH LNGVPCVVAV NRFPTDTDLE VVRVVELAAS YGVPAYQATH FTDGGIGAQD
LAKGVLQALE EPARDEFSFT YPDELSLTEK VEAVATRVYG AGQVTWDGKA RKRLARIERD
GYGTLPVCVA KTQYSFSTDP GLLGAPTGHE LRVREVRLSA GAGFVVVICG DMMTMPGLPT
RPAATRIDLA DDGTIIGLS