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Database: UniProt
Entry: U4L195_PYROM
LinkDB: U4L195_PYROM
Original site: U4L195_PYROM 
ID   U4L195_PYROM            Unreviewed;       269 AA.
AC   U4L195;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|ARBA:ARBA00038966};
DE            EC=6.3.3.2 {ECO:0000256|ARBA:ARBA00038966};
GN   ORFNames=PCON_05436 {ECO:0000313|EMBL:CCX05849.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX05849.1};
RN   [1] {ECO:0000313|EMBL:CCX05849.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX05849.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX05849.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
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; HF935274; CCX05849.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4L195; -.
DR   STRING; 1076935.U4L195; -.
DR   eggNOG; KOG3093; Eukaryota.
DR   OMA; DKWGIPT; -.
DR   OrthoDB; 5490047at2759; -.
DR   Proteomes; UP000018144; 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   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:CCX05849.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   269 AA;  29425 MW;  AE61E38DED116450 CRC64;
     MTSDLLLDST GVPTPRSITP MTVAPTLHTA KRALRTKVKG ILKTLPADSI RAQSDTILRT
     VLNLPEYKNA RSLSIYLSMP KGEVTTGALV TASLEAGKQV FVPYIHRQPP SHPIASSASL
     AASASAPPSL MDMLSLSSLS DFQGFQPDSW GIPTIPEDGR SERQDGLKAG LDLIIMPGVA
     FSEEFKRCGH GKGFYDYFLT RYNQARQAEE VKEEEASGVE TSQVRQRKMP VLVALALKEQ
     MVEEVPTDLS DWYMDVVVTG DGRCLRREA
//
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