ID W0EQN8_9BACT Unreviewed; 187 AA.
AC W0EQN8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN ORFNames=BARVI_02185 {ECO:0000313|EMBL:AHF11848.1};
OS Barnesiella viscericola DSM 18177.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF11848.1, ECO:0000313|Proteomes:UP000018901};
RN [1] {ECO:0000313|EMBL:AHF11848.1, ECO:0000313|Proteomes:UP000018901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007034; AHF11848.1; -; Genomic_DNA.
DR AlphaFoldDB; W0EQN8; -.
DR STRING; 880074.BARVI_02185; -.
DR KEGG; bvs:BARVI_02185; -.
DR PATRIC; fig|880074.11.peg.452; -.
DR eggNOG; COG0212; Bacteria.
DR HOGENOM; CLU_066245_2_2_10; -.
DR OrthoDB; 9801938at2; -.
DR Proteomes; UP000018901; 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:AHF11848.1};
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 4..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 128..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 187 AA; 21725 MW; 0AF816E89FBB0615 CRC64;
MLDKRQIRQE IKHRKQGITP DERERLSRQI CRAIESLPGF ERVVHLMLYH ALPDEVDTRP
LLSKWARDKQ LYLPIVDGDD LIVAPYAEGA MKQGAFHIWE PTGTTAIDPA RLEWIVVPGV
AFDRQMNRLG RGKGFYDRLL QQTPARKIGI CYGLQLVDEI PTEPHDMKMD LIVTENDIIY
KNDEIWH
//
