ID D7LBQ3_ARALL Unreviewed; 350 AA.
AC D7LBQ3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=methenyltetrahydrofolate cyclohydrolase {ECO:0000256|ARBA:ARBA00012776};
DE EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
GN ORFNames=ARALYDRAFT_482876 {ECO:0000313|EMBL:EFH56017.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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DR EMBL; GL348716; EFH56017.1; -; Genomic_DNA.
DR RefSeq; XP_002879758.1; XM_002879712.1.
DR AlphaFoldDB; D7LBQ3; -.
DR STRING; 81972.D7LBQ3; -.
DR EnsemblPlants; fgenesh2_kg.4__1936__AT2G38660.3; fgenesh2_kg.4__1936__AT2G38660.3; fgenesh2_kg.4__1936__AT2G38660.3.
DR Gramene; fgenesh2_kg.4__1936__AT2G38660.3; fgenesh2_kg.4__1936__AT2G38660.3; fgenesh2_kg.4__1936__AT2G38660.3.
DR eggNOG; KOG0089; Eukaryota.
DR HOGENOM; CLU_034045_1_2_1; -.
DR Proteomes; UP000008694; 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:SF10; BIFUNCTIONAL PROTEIN FOLD 1, 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:UP000008694}.
FT DOMAIN 64..179
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 182..347
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 350 AA; 37779 MW; A586FCB942B96349 CRC64;
MIARKALASA HTKAIRLTTR DVHCFSSILV SPPLVSLDLP ENWIPYSDPP PPVSFETEQK
TVVIDGNVIA EEIRTKISSE VRKMKKAVGK VPGLAVVLVG QQRDSQTYVR NKIKACEETG
IKSILAELPE DCTEGQILSI LKKFNEDTSI HGILVQLPLP QHLDESKILN MVRLEKDVDG
FHPLNVGNLA MRGREPLFVS CTPKGCVELL IRAGVEIAGK NAVVIGRSNI VGLPMSLLLQ
RHDATVSTVH AFTKDPEQIT RKADIVIAAA GIPSLVRGSW LKPGAVVIDV GTSPVEDSSC
EFGYRLVGDV CYEEALGVAS AITPVPGGVG PMTITMLLCN TLDAAKRIFL
//