FTHS_CLONN
ID FTHS_CLONN Reviewed; 556 AA.
AC A0PXN0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=NT01CX_1042;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61005.1; -; Genomic_DNA.
DR RefSeq; WP_011721153.1; NC_008593.1.
DR AlphaFoldDB; A0PXN0; -.
DR SMR; A0PXN0; -.
DR STRING; 386415.NT01CX_1042; -.
DR PRIDE; A0PXN0; -.
DR EnsemblBacteria; ABK61005; ABK61005; NT01CX_1042.
DR KEGG; cno:NT01CX_1042; -.
DR PATRIC; fig|386415.7.peg.158; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000008220; 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..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300519"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 60126 MW; 8BCA88252C288010 CRC64;
MKSDIEIAQS ANMKKIADIA KELGLGEDDI ELYGKYKCKI SLDVLKNKHN EADGKLILVT
AINPTPAGEG KSTITVGLGQ ALCKLHKKAV IALREPSLGP VFGIKGGAAG GGYSQVVPME
DINLHFTGDM HAITSANNLL AAAIDNHIHQ GNTLKIDSRR ILFKRVMDMN DRALRHIVVG
MGGKVNGFLR EDGFTITVAS EIMAILCLSN SLMDLKERFG NILVAYNLDG EPIYCKDLNV
HGAMAMLMKD AIKPNLVQTL ENTPAIIHGG PFANIAHGCN SILATKMAMK LGDYAITEAG
FGADLGAEKF LDIKCRYGNL KPDCIVVVAT IRALKHHGGV SKDELSTPDI EALSKGVSNL
QKQIENMKKY GVPVVVAINK FITDSDEEVE FIKEFCDKQG VEVALAEVWE KGGEGGIALA
EKVINVLDTQ KSNFKCLYDE KLSIKEKMDI IAREIYGASG VDYDKSAEKD IKDIEKLGLD
KLPICVAKTQ YSLSDNPSLL GKPEDFRVNV REVKVSNGAG FIVVLTGNIM TMPGLPKVPA
ANKMDILEGG TIQGLF
