ID J4UN66_BEAB2 Unreviewed; 239 AA.
AC J4UN66;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-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=BBA_04397 {ECO:0000313|EMBL:EJP66457.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP66457.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP66457.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66457.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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; JH725159; EJP66457.1; -; Genomic_DNA.
DR RefSeq; XP_008597716.1; XM_008599494.1.
DR AlphaFoldDB; J4UN66; -.
DR STRING; 655819.J4UN66; -.
DR GeneID; 19887409; -.
DR HOGENOM; CLU_066245_2_1_1; -.
DR InParanoid; J4UN66; -.
DR OrthoDB; 5490047at2759; -.
DR Proteomes; UP000002762; 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; 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:EJP66457.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006806-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762}.
FT BINDING 9..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
FT BINDING 170..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR006806-1"
SQ SEQUENCE 239 AA; 26110 MW; DEB3640527B04C8C CRC64;
MATPVAAAKQ QLRTLIKKRL ASLSQDAVQA QSHAVFDTLQ ASKQYREAKR ISIYLAMPAA
EVQTDAIVRH ALNAGKQVFV PYLHRSTLSE PGTPARIMDM VQLRSIQDYE SLGRDRWGIP
SIDDAAVAGR ERILGDSPGK FGPSPATLDL MLVPGVAFDS DAEVGAGIRR LGHGKGFYDF
FLNRYFARVA EHGGHGESLR LIGLALTEQW LEPGDGQVPM GMFDRRLHSL ILGSGETKT
//
