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Database: UniProt
Entry: A0A212F9K8_DANPL
LinkDB: A0A212F9K8_DANPL
Original site: A0A212F9K8_DANPL 
ID   A0A212F9K8_DANPL        Unreviewed;       314 AA.
AC   A0A212F9K8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=methenyltetrahydrofolate cyclohydrolase {ECO:0000256|ARBA:ARBA00012776};
DE            EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
GN   ORFNames=KGM_215394 {ECO:0000313|EMBL:OWR50410.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR50410.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR50410.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR50410.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWR50410.1}.
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DR   EMBL; AGBW02009565; OWR50410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212F9K8; -.
DR   STRING; 278856.A0A212F9K8; -.
DR   KEGG; dpl:KGM_215394; -.
DR   eggNOG; KOG0089; Eukaryota.
DR   InParanoid; A0A212F9K8; -.
DR   Proteomes; UP000007151; 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; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007151}.
FT   DOMAIN          20..135
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          138..310
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   314 AA;  34242 MW;  84074708C93F6CB4 CRC64;
     MRSHTYNESL GTARIMARIL DGKALAKEIK DEVKIEINNW IRNGNPAPTL RCIIVGEDPA
     SHTYVRNKIQ AAREVGIEAE TIRYDANLTE EALMSIIDSL NKDKNINGIL VQLPLPNSID
     ERRVCNALAP EKDVDGFHIT NVGQLCLDMP TIVPATALAV VEMLRRFKID TFGRNTVVIG
     RSKNVGMPIA MMLHSDGRHD SGLGMDSTVT ICHRHTPADQ LEFYCRHADI IVSATGLPKL
     IKADMVKPGA TIIDVGITRV TDESGKTKLV GDVDYDEVVK VAGAITPVPG GVGPMTVAML
     MKNTLQAAQH NSFK
//
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