ID A0A0L7QNI5_9HYME Unreviewed; 339 AA.
AC A0A0L7QNI5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=methenyltetrahydrofolate cyclohydrolase {ECO:0000256|ARBA:ARBA00012776};
DE EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
GN ORFNames=WH47_07784 {ECO:0000313|EMBL:KOC60202.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC60202.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC60202.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC60202.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:195366; EC=3.5.4.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036357};
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DR EMBL; KQ414851; KOC60202.1; -; Genomic_DNA.
DR RefSeq; XP_017795540.1; XM_017940051.1.
DR AlphaFoldDB; A0A0L7QNI5; -.
DR STRING; 597456.A0A0L7QNI5; -.
DR EnsemblMetazoa; XM_017940051.1; XP_017795540.1; LOC108576974.
DR GeneID; 108576974; -.
DR OrthoDB; 5386942at2759; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099:SF11; BIFUNCTIONAL METHYLENETETRAHYDROFOLATE DEHYDROGENASE_CYCLOHYDROLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KOC60202.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825}.
FT DOMAIN 31..146
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 151..320
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 339 AA; 37417 MW; 550916D6C8D0AD28 CRC64;
MSLWKKVLQI TFHWPVRQLH TSKVQQKAVI INGKQIADEI QNELKTTVHT WISDNRKRPK
LVAIIVGNNP ASKVYVARKM EAAKFIGIEN YTIHLEQNRS QQDLIKEINN LNEDETVDGV
LVQLPLTKHM NEHKVCQAIA SNKDVDGFNL ENLGSLALNS NGIVPATALA VKELIIRSNI
DTFGKNAVVI GRSKHVGLPI ALLLHADSKG ETSALDMTTT ICHRHTPHTE LEKFTKLADV
VVAAAGIPGL ITKEMIKPGA CIIDVGITRV KMDNKFKLVG DVDFENVKEI AGHITPVPGG
VGPMTVTMLM KNTILAAKRN YENSKQFELN KTEAPILMV
//
