ID A0A1M4X8U2_9FIRM Unreviewed; 189 AA.
AC A0A1M4X8U2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN ORFNames=SAMN02746064_01432 {ECO:0000313|EMBL:SHE89825.1};
OS Alkalibacter saccharofermentans DSM 14828.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibacter.
OX NCBI_TaxID=1120975 {ECO:0000313|EMBL:SHE89825.1, ECO:0000313|Proteomes:UP000184251};
RN [1] {ECO:0000313|EMBL:SHE89825.1, ECO:0000313|Proteomes:UP000184251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14828 {ECO:0000313|EMBL:SHE89825.1,
RC ECO:0000313|Proteomes:UP000184251};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQTU01000009; SHE89825.1; -; Genomic_DNA.
DR RefSeq; WP_073270576.1; NZ_FQTU01000009.1.
DR AlphaFoldDB; A0A1M4X8U2; -.
DR STRING; 1120975.SAMN02746064_01432; -.
DR OrthoDB; 9801938at2; -.
DR Proteomes; UP000184251; Unassembled WGS sequence.
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:SHE89825.1};
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:UP000184251}.
FT BINDING 3..7
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 134..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 189 AA; 21593 MW; B7C42E6B0445C88C CRC64;
MDKKSLREQI INKRTGFDSN YVKNISKRIF GTIKKMDIYQ KSDVIMIYVS FMNEINTHDF
IIDALKEGKT VITPICNNEN KTLILAKTFE FPKGFKKTKY GILEIPKTKA VVVDIKDIDL
IITPGLAFTW SGKRLGYGGG FYDRLLSEKR SDTSTVCPAY KEFVLNDLPT DEHDVGVDYL
VTDEEIIKC
//