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Database: UniProt
Entry: A0A1K2IBL7_9FLAO
LinkDB: A0A1K2IBL7_9FLAO
Original site: A0A1K2IBL7_9FLAO 
ID   A0A1K2IBL7_9FLAO        Unreviewed;       187 AA.
AC   A0A1K2IBL7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279};
DE            EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279};
GN   ORFNames=SAMN05428642_101564 {ECO:0000313|EMBL:SFZ89791.1};
OS   Flaviramulus basaltis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flaviramulus.
OX   NCBI_TaxID=369401 {ECO:0000313|EMBL:SFZ89791.1, ECO:0000313|Proteomes:UP000182544};
RN   [1] {ECO:0000313|EMBL:SFZ89791.1, ECO:0000313|Proteomes:UP000182544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18180 {ECO:0000313|EMBL:SFZ89791.1,
RC   ECO:0000313|Proteomes:UP000182544};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FPKV01000001; SFZ89791.1; -; Genomic_DNA.
DR   RefSeq; WP_072400227.1; NZ_FPKV01000001.1.
DR   AlphaFoldDB; A0A1K2IBL7; -.
DR   STRING; 369401.SAMN05428642_101564; -.
DR   OrthoDB; 9801938at2; -.
DR   Proteomes; UP000182544; 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:SFZ89791.1};
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:UP000182544}.
FT   BINDING         3..7
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   187 AA;  21757 MW;  F9D89ED66F92954B CRC64;
     MTKTELRKTY KNLRNKLSQN QIEDFSLAIS NQLLKLPVWD YSFYHIFLSI EEHNEVNTDY
     ILNILSGKDK NILISKSDFE TGDMIHYLLT DNTVIKKNTY NIPEPIDGIE ITDDKIEVVF
     IPLLAFDKQG NRVGYGKGFY DRFLSKCNTE TIKIGLSFFE AENIILDTIE SDVKLDYCVT
     PKKVYEF
//
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