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Database: UniProt
Entry: E1QZZ2_OLSUV
LinkDB: E1QZZ2_OLSUV
Original site: E1QZZ2_OLSUV 
ID   E1QZZ2_OLSUV            Unreviewed;       199 AA.
AC   E1QZZ2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   OrderedLocusNames=Olsu_0843 {ECO:0000313|EMBL:ADK67956.1};
OS   Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS   NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK67956.1, ECO:0000313|Proteomes:UP000000333};
RN   [1] {ECO:0000313|EMBL:ADK67956.1, ECO:0000313|Proteomes:UP000000333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC   VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX   PubMed=21304694; DOI=10.4056/sigs.1082860;
RA   Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA   Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL   Stand. Genomic Sci. 3:76-84(2010).
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; CP002106; ADK67956.1; -; Genomic_DNA.
DR   RefSeq; WP_013251708.1; NZ_JQCO01000001.1.
DR   AlphaFoldDB; E1QZZ2; -.
DR   STRING; 633147.Olsu_0843; -.
DR   GeneID; 78512260; -.
DR   KEGG; ols:Olsu_0843; -.
DR   PATRIC; fig|633147.7.peg.705; -.
DR   eggNOG; COG0212; Bacteria.
DR   HOGENOM; CLU_066245_2_2_11; -.
DR   OrthoDB; 3242798at2; -.
DR   Proteomes; UP000000333; 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:ADK67956.1};
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:UP000000333}.
FT   BINDING         11..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         144..152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ   SEQUENCE   199 AA;  21374 MW;  7C8F664DCDA88AB0 CRC64;
     MASSCGEDAS KNALRDAYLT LRASLTPRQR GRLEAQVVRH LTELEAYRSA DLLLAYVAYR
     DEMDTRAMCE RAWADGKSVA LPRCEGGEQS LAFYVVDTLE GLAPGARGAL EPVVDDGDVS
     LDPTALQTSV CLVPGLVFDA AGYRVGYGAG YYDNFLAGYV GTKVGVVHAM QVSGNPLPHD
     EHDVAVDVLV SDGAIWMCR
//
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