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Database: UniProt
Entry: F0Z185_9CLOT
LinkDB: F0Z185_9CLOT
Original site: F0Z185_9CLOT 
ID   F0Z185_9CLOT            Unreviewed;       556 AA.
AC   F0Z185;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
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   ORFNames=HMPREF0240_02867 {ECO:0000313|EMBL:EGB92187.1};
OS   Clostridium sp. D5.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=556261 {ECO:0000313|EMBL:EGB92187.1, ECO:0000313|Proteomes:UP000003978};
RN   [1] {ECO:0000313|EMBL:EGB92187.1, ECO:0000313|Proteomes:UP000003978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D5 {ECO:0000313|EMBL:EGB92187.1,
RC   ECO:0000313|Proteomes:UP000003978};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA   Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA   Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA   Sibley C.D., White A.P., Crowley S., Surette M.G., Strauss J.C.,
RA   Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium sp. D5.";
RL   Submitted (MAR-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}.
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DR   EMBL; GL870814; EGB92187.1; -; Genomic_DNA.
DR   RefSeq; WP_009004167.1; NZ_GL870814.1.
DR   AlphaFoldDB; F0Z185; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000003978; 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:EGB92187.1};
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:UP000003978}.
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   556 AA;  60313 MW;  6A113B294E85A560 CRC64;
     MKTDIQIAQE AELLHIRDVA AKIGIEEEDL EFYGKYKAKL SDDLWDKIKD REDGKLVLVT
     AINPTPAGEG KTTTTVGLGQ AMAKLNKKAL IALREPSLGP CFGIKGGAAG GGYAQVVPME
     DLNLHFTGDF HAITSANNLL AAMLDNHIQQ GNVLGIDPRQ VVWKRCLDMN DRVLRNTVVG
     LGNKMDGMVR EDHFVITVAS EIMAILCLAD DLADLKRRLG RIIVAYNFAG DPVTADDLQA
     TGAMTALLKD AIKPNIIQTL EHTPALVHGG PFANIAHGCN SVRATKMALK ISDITITEAG
     FGADLGAEKF LDIKCRKAGL KPDAVVLVAT VRALKYNGGV AKSDLGEENL EALEKGIVNL
     EKHIENIQKY DVPVIVTLNS FVTDTEAEND YIRRFCEERG CEFALSEVWE KGGDGGVMLA
     EKVLETLEKK ESYFHPLYAD ELSLKEKIET IAKEIYGARG VVYEPAAEKQ LAKIEAMGFG
     AFPVCMAKNQ YSLSDDAKKL GRPENFDIHI REVYVSAGAG FVVALTGAIM TMPGLPKVPA
     ANNIDVTEDG KITGLF
//
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