MTDC_CHICK
ID MTDC_CHICK Reviewed; 337 AA.
AC Q5ZKA5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial;
DE Includes:
DE RecName: Full=NAD-dependent methylenetetrahydrofolate dehydrogenase;
DE EC=1.5.1.15 {ECO:0000250|UniProtKB:P18155};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase;
DE EC=3.5.4.9 {ECO:0000250|UniProtKB:P18155};
DE Flags: Precursor;
GN Name=MTHFD2; ORFNames=RCJMB04_12b8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Although its dehydrogenase activity is NAD-specific, it can
CC also utilize NADP at a reduced efficiency.
CC {ECO:0000250|UniProtKB:P13995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-
CC methenyltetrahydrofolate + NADH; Xref=Rhea:RHEA:22892,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.5.1.15;
CC Evidence={ECO:0000250|UniProtKB:P18155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:57455; EC=3.5.4.9;
CC Evidence={ECO:0000250|UniProtKB:P18155};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18155};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
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DR EMBL; AJ720179; CAG31838.1; -; mRNA.
DR RefSeq; NP_001026531.1; NM_001031360.1.
DR AlphaFoldDB; Q5ZKA5; -.
DR SMR; Q5ZKA5; -.
DR BioGRID; 685886; 1.
DR STRING; 9031.ENSGALP00000022034; -.
DR PaxDb; Q5ZKA5; -.
DR GeneID; 426126; -.
DR KEGG; gga:426126; -.
DR CTD; 10797; -.
DR VEuPathDB; HostDB:geneid_426126; -.
DR eggNOG; KOG0089; Eukaryota.
DR InParanoid; Q5ZKA5; -.
DR OrthoDB; 1004679at2759; -.
DR PhylomeDB; Q5ZKA5; -.
DR PRO; PR:Q5ZKA5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; ISS:UniProtKB.
DR GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0042301; F:phosphate ion binding; ISS:UniProtKB.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_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 Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 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; NADP;
KW One-carbon metabolism; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..337
FT /note="Bifunctional methylenetetrahydrofolate
FT dehydrogenase/cyclohydrolase, mitochondrial"
FT /id="PRO_0000042885"
FT BINDING 79..83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 195..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 304..308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13995"
SQ SEQUENCE 337 AA; 36411 MW; CA3B321FC58F32CC CRC64;
MATALCPLRA LGQTAFRPRT RRLHLSAPRA DAVVISGRKL ARQIRQEARH EVEQWVAAGN
KRPHLSVVLV GENPASHSYV LNKTKAAADV GISSETILKP ASITEEELLD LISKLNNDAN
VDGLLVQLPL PEHIDERKIC NAVTPDKDVD GFHVINVGRM CLDQYSMLPA TPWGVWEIIK
RTGIPTLGKN VVVAGRSKNV GMPIAMLLHT DGRHERPGGD ATVTISHRYT PKEQLKQHTI
RADIVVAAAG IPNLITADMI KEGAAVIDVG ITRVQDPITA KSRLVGDVDF EGVKKKASYI
TPVPGGVGPM TVAMLMKNTI IAAKKLLKPK ALEALTA
