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Database: UniProt
Entry: A0A1W5DCI2_9LECA
LinkDB: A0A1W5DCI2_9LECA
Original site: A0A1W5DCI2_9LECA 
ID   A0A1W5DCI2_9LECA        Unreviewed;       243 AA.
AC   A0A1W5DCI2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|ARBA:ARBA00038966};
DE            EC=6.3.3.2 {ECO:0000256|ARBA:ARBA00038966};
OS   Lasallia pustulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC   Lasallia.
OX   NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM40796.1, ECO:0000313|Proteomes:UP000192927};
RN   [1] {ECO:0000313|Proteomes:UP000192927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma R., Thines M.;
RL   Submitted (MAR-2017) 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|ARBA:ARBA00036539};
CC   -!- SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase
CC       family. {ECO:0000256|ARBA:ARBA00010638}.
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DR   EMBL; FWEW01003741; SLM40796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W5DCI2; -.
DR   OrthoDB; 5490047at2759; -.
DR   Proteomes; UP000192927; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; 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   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; 2.
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:SLM40796.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR006806-1}.
FT   BINDING         12..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT   BINDING         173..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ   SEQUENCE   243 AA;  27089 MW;  6B04002550E6EE85 CRC64;
     MDDDMTTLKI AKQELRKTLR RRLSHVPTEA VTQQSRAIVD ILFSLPEYQA AQRISIYLSM
     PSGEVSTVPI VQDALRHGKK VFVPYIHHLA TPEPGGARKV MDMVSLLDWA DYEALERDAW
     GIPTPTLDSI ARRERCLGDA GSLGGEQGRG EGSGWGLDLV VMPGMGFDRG LRRLGHGKGF
     YDFFLQRYQH KTTMTEEQGN RKMPLLVGLA LEEQLLPPNA EVPTNNQDWP LNALIVGDGT
     LIR
//
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