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Database: UniProt
Entry: G0VPU5_MEGEL
LinkDB: G0VPU5_MEGEL
Original site: G0VPU5_MEGEL 
ID   G0VPU5_MEGEL            Unreviewed;       188 AA.
AC   G0VPU5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   ORFNames=MELS_1252 {ECO:0000313|EMBL:CCC73473.1};
OS   Megasphaera elsdenii DSM 20460.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC73473.1, ECO:0000313|Proteomes:UP000010111};
RN   [1] {ECO:0000313|EMBL:CCC73473.1, ECO:0000313|Proteomes:UP000010111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC73473.1,
RC   ECO:0000313|Proteomes:UP000010111};
RX   PubMed=21914887; DOI=10.1128/JB.05861-11;
RA   Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT   "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL   J. Bacteriol. 193:5578-5579(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; HE576794; CCC73473.1; -; Genomic_DNA.
DR   RefSeq; WP_014016204.1; NZ_CP027570.1.
DR   AlphaFoldDB; G0VPU5; -.
DR   STRING; 1064535.MELS_1252; -.
DR   KEGG; med:MELS_1252; -.
DR   eggNOG; COG0212; Bacteria.
DR   HOGENOM; CLU_066245_1_1_9; -.
DR   Proteomes; UP000010111; 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:CCC73473.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010111}.
FT   BINDING         4..8
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         132..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ   SEQUENCE   188 AA;  20559 MW;  23F864EE0AA7F3DE CRC64;
     MLSKKELRKA MNDRLHQLTE GEKAAASAAV CAHLAALPQY QQARSIMAFL HMPDEVSLDG
     LIQQALADGK EVYVPVCVDK QRIEGRRLYT LEQAVCGAYG IRTAPPDNPR IEADELDVIF
     VPGLAFDAKG HRLGHGAAYY DRFLAGKGRA AAIAAAWDVQ LVPDVPVEAH DIVMTDIVTD
     KQHLVIHP
//
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