ID M3Y246_MUSPF Unreviewed; 572 AA.
AC M3Y246;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN Name=ME1 {ECO:0000313|Ensembl:ENSMPUP00000005397.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000005397.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000005397.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR EMBL; AEYP01081691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01081698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004773664.1; XM_004773607.2.
DR AlphaFoldDB; M3Y246; -.
DR STRING; 9669.ENSMPUP00000005397; -.
DR Ensembl; ENSMPUT00000005486.1; ENSMPUP00000005397.1; ENSMPUG00000005436.1.
DR GeneID; 101691209; -.
DR KEGG; mpuf:101691209; -.
DR CTD; 4199; -.
DR eggNOG; KOG1257; Eukaryota.
DR GeneTree; ENSGT00950000183134; -.
DR HOGENOM; CLU_011405_5_0_1; -.
DR InParanoid; M3Y246; -.
DR OMA; QIVNHMV; -.
DR OrthoDB; 1069499at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:Ensembl.
DR GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:Ensembl.
DR GO; GO:0006108; P:malate metabolic process; IEA:Ensembl.
DR GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR GO; GO:0006739; P:NADP metabolic process; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:1902031; P:regulation of NADP metabolic process; IEA:Ensembl.
DR CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF17; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426}.
FT DOMAIN 79..260
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 270..522
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 245
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 246
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 269
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 453
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 572 AA; 63989 MW; F2448D9E5407743A CRC64;
MEPAAPRRRH THQRGYAATR NPHLNKDLAF TLEERQQLNI HGLLPPCFIS QDIQVLRVIK
NFERLTSDFD RYLLLMDLQD RNEKLFYSVL MSDIEKFMPI VYTPTVGLAC QQYSLAFRKP
RGLFISIHDR GHIASVLNAW PEDVIKAIVV TDGERILGLG DLGCNGMGIP VGKLALYTAC
GGMNPQECLP VTLDVGTENE DLLKDPLYIG LRQRRVRGPE YDEFLDEFME AVSSKYGMNC
LIQFEDFANI NAFRLLKKYQ NQYCTFNDDI QGTASVAVAG ILAALRITKN KLSDQTVLFQ
GAGEAALGIA HLIVMAMQKE GLPKEKAMKK IWLVDSKGLI VKGRAALTQE KEEFAHEHEE
MKNLEAIVQE IKPTALIGVA AIGGAFSEQI LKDMAAFNER PIIFALSNPT SKAECTAEQC
YKLTKGRAIF ASGSPFDPVT LSNGRTLYPG QGNNSYVFPG VALGVVACGL RHITDKIFLT
TAEVIAQEVS DKHLEEGRLY PPLNTIRDVS LKIAAKIVKD AYQEKTATVY PEPPNKEEFV
RSQMYNTDYD QILPDCYSWP KEAQKIQTKL DQ
//
