ID   MTDC_BOVIN              Reviewed;         350 AA.
AC   Q0P5C2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial;
DE   Includes:
DE     RecName: Full=NAD-dependent methylenetetrahydrofolate dehydrogenase;
DE              EC=1.5.1.15;
DE   Includes:
DE     RecName: Full=Methenyltetrahydrofolate cyclohydrolase;
DE              EC=3.5.4.9;
DE   Flags: Precursor;
GN   Name=MTHFD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Placenta;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NAD(+) =
CC       5,10-methenyltetrahydrofolate + NADH.
CC   -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10-
CC       formyltetrahydrofolate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- MISCELLANEOUS: This NAD-dependent bifunctional enzyme has very
CC       different kinetic properties than the larger NADP-dependent
CC       trifunctional enzyme and is unique in that it requires formation
CC       of an enzyme-magnesium complex to allow binding of NAD (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family.
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DR   EMBL; BC120249; AAI20250.1; -; mRNA.
DR   IPI; IPI00712161; -.
DR   RefSeq; NP_001069223.1; -.
DR   UniGene; Bt.6685; -.
DR   Ensembl; ENSBTAG00000004881; Bos taurus.
DR   GeneID; 517539; -.
DR   KEGG; bta:517539; -.
DR   HOVERGEN; Q0P5C2; -.
DR   OMA; Q0P5C2; HSKTRDL.
DR   BRENDA; 1.5.1.15; 251.
DR   BRENDA; 3.5.4.9; 251.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase act...; IEA:EC.
DR   GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NA...; IEA:EC.
DR   GO; GO:0009396; P:folic acid and derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   ProDom; PD002300; THFDhg/Cyc_hydro; 1.
DR   PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Mitochondrion; Multifunctional enzyme; NAD;
KW   One-carbon metabolism; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     35       Mitochondrion (By similarity).
FT   CHAIN        36    350       Bifunctional methylenetetrahydrofolate
FT                                dehydrogenase/cyclohydrolase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000305902.
SQ   SEQUENCE   350 AA;  37767 MW;  D71A67DFE1FEE05F CRC64;
     MAAASFITSL VTRLLRSAQS GRLHQRPFHL SAVRNEAVVI SGRKLAEQIK QEVRQEVEEW
     VASGNKRPHL SVVLVGENPA SQSYVLNKTR AAASVGINSE TILKPASISE EELLNLINKL
     NNDDNVDGLL VQLPLPEHID ERKVCNAVSP DKDVDGFHVI NVGRMCLDQC SMLPATPWGV
     WEIIKRTGIP TLGKNVVVAG RSKNVGMPIA MLLHTDGAHE RPGGDATVTI SHRYTPKEEL
     KKHTALADIV ISAAGIPNLI TADMIKEGAA VIDVGINRIQ DPITAKPKLV GDVDFEGVKK
     KAGYITPVPG GVGPMTVAML MKNTIIAAKK VLRLEEQEVL KSKELGVASN
//