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Database: UniProt
Entry: A0A1M4X8U2_9FIRM
LinkDB: A0A1M4X8U2_9FIRM
Original site: A0A1M4X8U2_9FIRM 
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
//
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