ID Q5SHW9_THET8 Unreviewed; 184 AA.
AC Q5SHW9;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN OrderedLocusNames=TTHA1611 {ECO:0000313|EMBL:BAD71434.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD71434.1, ECO:0000313|Proteomes:UP000000532};
RN [1] {ECO:0007829|PDB:1WKC}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
RA Yanai H., Tsuge H., Utsunomiya H., Yokoyama S., Kuramitsu S.;
RT "Crystal structure of a 5-formyltetrahydrofolate cycloligase-related
RT protein from Thermus thermophilus HB8.";
RL Submitted (MAY-2004) to the PDB data bank.
RN [2] {ECO:0000313|EMBL:BAD71434.1, ECO:0000313|Proteomes:UP000000532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; AP008226; BAD71434.1; -; Genomic_DNA.
DR RefSeq; WP_011228804.1; NC_006461.1.
DR RefSeq; YP_144877.1; NC_006461.1.
DR PDB; 1WKC; X-ray; 1.70 A; A=1-184.
DR PDBsum; 1WKC; -.
DR AlphaFoldDB; Q5SHW9; -.
DR SMR; Q5SHW9; -.
DR EnsemblBacteria; BAD71434; BAD71434; BAD71434.
DR GeneID; 3169785; -.
DR KEGG; ttj:TTHA1611; -.
DR PATRIC; fig|300852.9.peg.1581; -.
DR eggNOG; COG0212; Bacteria.
DR HOGENOM; CLU_066245_1_1_0; -.
DR EvolutionaryTrace; Q5SHW9; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1WKC};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR006806-
KW 1}; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000532}.
FT BINDING 3..7
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 119..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 184 AA; 20334 MW; ED241AD79BEF22B2 CRC64;
MTKAELRRRA RAAWRRLDLK ALSRAVGAAL LPWLRERGFR HILLYHPLPH ELNLLPLMEA
YPARYYLPKV AGKGLTVHPF GPLAPGPFGL LEPTTPPEDP RVLDLVVVPG LAFDREGYRL
GHGQGFYDRF LKEVRAATVG VVPQALLFPA LPRDPWDVPV DHLATEAGVE AVKRPAPGPG
GLLD
//
