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Database: UniProt
Entry: D5WSC1_KYRT2
LinkDB: D5WSC1_KYRT2
Original site: D5WSC1_KYRT2 
ID   D5WSC1_KYRT2            Unreviewed;       200 AA.
AC   D5WSC1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   OrderedLocusNames=Btus_0229 {ECO:0000313|EMBL:ADG05006.1};
OS   Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX   NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG05006.1, ECO:0000313|Proteomes:UP000002368};
RN   [1] {ECO:0000313|Proteomes:UP000002368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Bacillus tusciae DSM 2912.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG05006.1, ECO:0000313|Proteomes:UP000002368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX   PubMed=22180816; DOI=10.4056/sigs.2144922;
RA   Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA   Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA   Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA   Hugenholtz P., Eisen J.A.;
RT   "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT   tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT   gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT   Alicyclobacillaceae da Costa and Rainey, 2010.";
RL   Stand. Genomic Sci. 5:121-134(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-formyl-5,6,7,8-tetrahydrofolate + ATP = (6R)-5,10-
CC         methenyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:10488,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57455,
CC         ChEBI:CHEBI:57457, ChEBI:CHEBI:456216; EC=6.3.3.2;
CC         Evidence={ECO:0000256|RuleBase:RU361279};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361279};
CC   -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC       family. {ECO:0000256|ARBA:ARBA00010638, ECO:0000256|RuleBase:RU361279}.
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DR   EMBL; CP002017; ADG05006.1; -; Genomic_DNA.
DR   RefSeq; WP_013074299.1; NC_014098.1.
DR   AlphaFoldDB; D5WSC1; -.
DR   STRING; 562970.Btus_0229; -.
DR   KEGG; bts:Btus_0229; -.
DR   eggNOG; COG0212; Bacteria.
DR   HOGENOM; CLU_066245_1_1_9; -.
DR   OMA; GIVFDFA; -.
DR   Proteomes; UP000002368; Chromosome.
DR   GO; GO:0030272; F:5-formyltetrahydrofolate cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR   InterPro; IPR002698; FTHF_cligase.
DR   InterPro; IPR024185; FTHF_cligase-like_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02727; MTHFS_bact; 1.
DR   PANTHER; PTHR23407:SF1; 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   PANTHER; PTHR23407; ATPASE INHIBITOR/5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE; 1.
DR   Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR   PIRSF; PIRSF006806; FTHF_cligase; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR006806-
KW   1}; Ligase {ECO:0000313|EMBL:ADG05006.1};
KW   Magnesium {ECO:0000256|RuleBase:RU361279};
KW   Metal-binding {ECO:0000256|RuleBase:RU361279};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006806-1}.
FT   BINDING         3..7
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         129..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ   SEQUENCE   200 AA;  21939 MW;  156D230518C417E3 CRC64;
     MDKGAWRRRL LQWRDDLGAR DREKREAALA AWATRWLGGM PPGILMAYAA IRSEVNLKSV
     VEWAWNHGWT VAFPRVEESH RISAVAADSW EALSPGAFGI PEPTGPALSP GDLDVIVVPG
     AAFDRLGRRL GYGQGFYDRF LPQVPQAKVV GAAFAEQWVD ALPADPHDVP VQYVLTEYGV
     WSVQDRGFVD LGGGTTGERG
//
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