MTD2L_CALJA
ID MTD2L_CALJA Reviewed; 347 AA.
AC F6ZFR0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial {ECO:0000250|UniProtKB:D3ZUA0};
DE AltName: Full=NADP-dependent methylenetetrahydrofolate dehydrogenase 2-like protein {ECO:0000250|UniProtKB:D3ZUA0};
DE Short=MTHFD2-like {ECO:0000250|UniProtKB:D3ZUA0};
DE Includes:
DE RecName: Full=NAD-dependent methylenetetrahydrofolate dehydrogenase {ECO:0000250|UniProtKB:D3ZUA0};
DE EC=1.5.1.15 {ECO:0000250|UniProtKB:D3ZUA0};
DE EC=1.5.1.5 {ECO:0000250|UniProtKB:D3ZUA0};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000250|UniProtKB:D3ZUA0};
DE EC=3.5.4.9 {ECO:0000250|UniProtKB:D3ZUA0};
GN Name=MTHFD2L {ECO:0000250|UniProtKB:D3ZUA0};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional mitochondrial folate-interconverting enzyme that
CC has both NAD/NADP-dependent methylenetetrahydrofolate dehydrogenase and
CC methenyltetrahydrofolate cyclohydrolase activities.
CC {ECO:0000250|UniProtKB:D3ZUA0}.
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:D3ZUA0};
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:D3ZUA0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.5;
CC Evidence={ECO:0000250|UniProtKB:D3ZUA0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:D3ZUA0};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000250|UniProtKB:D3ZUA0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:D3ZUA0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:D3ZUA0}; Matrix side
CC {ECO:0000250|UniProtKB:D3ZUA0}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000305}.
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DR EMBL; ACFV01093585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACFV01093586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACFV01093587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ACFV01093588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002745776.1; XM_002745730.3.
DR AlphaFoldDB; F6ZFR0; -.
DR SMR; F6ZFR0; -.
DR STRING; 9483.ENSCJAP00000025515; -.
DR Ensembl; ENSCJAT00000093762; ENSCJAP00000073826; ENSCJAG00000013883.
DR GeneID; 100389511; -.
DR KEGG; cjc:100389511; -.
DR CTD; 441024; -.
DR eggNOG; KOG0089; Eukaryota.
DR GeneTree; ENSGT00940000160901; -.
DR HOGENOM; CLU_034045_0_1_1; -.
DR InParanoid; F6ZFR0; -.
DR OMA; CKVITAE; -.
DR OrthoDB; 1004679at2759; -.
DR TreeFam; TF323998; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000008225; Chromosome 3.
DR Bgee; ENSCJAG00000013883; Expressed in liver and 6 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; ISS:UniProtKB.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; Magnesium;
KW Membrane; Methionine biosynthesis; Mitochondrion;
KW Mitochondrion inner membrane; Multifunctional enzyme; NAD;
KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..347
FT /note="Bifunctional methylenetetrahydrofolate
FT dehydrogenase/cyclohydrolase 2, mitochondrial"
FT /id="PRO_0000413327"
FT BINDING 98..102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 214..216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P13995"
FT BINDING 323..327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13995"
SQ SEQUENCE 347 AA; 37342 MW; 0A425A0D6AF2797C CRC64;
MTVPARGFLL LRGRLGRVPA LGRSTAPPVR APGGPRSAFR GFRSSGVRHE AVIISGTEMA
KHIQKEIKQG VESWISLGNR RPHLSIILVG DNPASHTYVR NKIRAASAVG ICSELILKPK
DVSQEELLDI TDQLNMDPRV SGILVQLPLP DHVDERMICN GIAPEKDVDG FHIINIGRLC
LDQHSLIPAT ASAVWEIITR TGIQTFGKNV VVAGRSKNVG MPIAMLLHTD GEHERPGGDA
TVTIAHRYTP KEQLKTHTQL ADVIIVAAGI PKLITSDMVK EGAAVIDVGI NYVHDPVTGK
TKLVGDVDFE AVKKKAGFIT PVPGGVGPMT VAMLLKNTLL AAKKIIY
