ID A0A3Q1F132_9TELE Unreviewed; 338 AA.
AC A0A3Q1F132;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=methenyltetrahydrofolate cyclohydrolase {ECO:0000256|ARBA:ARBA00012776};
DE EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000011311.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000011311.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q1F132; -.
DR STRING; 80966.ENSAPOP00000011311; -.
DR Ensembl; ENSAPOT00000018868.1; ENSAPOP00000011311.1; ENSAPOG00000013845.1.
DR GeneTree; ENSGT00940000164825; -.
DR InParanoid; A0A3Q1F132; -.
DR OrthoDB; 5386942at2759; -.
DR Proteomes; UP000257200; Unplaced.
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:SF15; 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 One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT DOMAIN 33..148
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 151..323
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 338 AA; 36755 MW; C149A43AB60CBA6D CRC64;
MAAVRTLRKL CQHSQHQVCK LHTSASRHEA VVISGKKLAR QIREEAQVDV EKWVLAGHRR
PHLSVVLVGD NPASHSYVLN KTRAAADVGI SSETILKHSD ISEEELLDLI YKLNADHRVD
GLLVQLPLPD HIDERTICNA VSPAKDVDGF HVVNVGRMCL DQSTMLPATP WGVWEIIKRT
GIPTLGKNVV VAGRSKNVGM PIAMLLHTDG RHERPGGDAT VTISHRYTPK DQLRQHTKIA
DIIVAAAGIP NLITADMIKE GAAVIDVGIN RVQDPVTGKN RLVGDVDFEG VRQKAGFITP
VPGGVGPMTV AMLMKNTIKA AKNVLLFPPE RIRMAAAS
//
