ID A0A2K5VE13_MACFA Unreviewed; 547 AA. AC A0A2K5VE13; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 2. DT 29-MAY-2024, entry version 26. DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426}; GN Name=ME2 {ECO:0000313|Ensembl:ENSMFAP00000022999.2}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000022999.2, ECO:0000313|Proteomes:UP000233100}; RN [1] {ECO:0000313|Ensembl:ENSMFAP00000022999.2, ECO:0000313|Proteomes:UP000233100} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMFAP00000022999.2} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the malic enzymes family. CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A2K5VE13; -. DR Ensembl; ENSMFAT00000031132.2; ENSMFAP00000022999.2; ENSMFAG00000004061.2. DR VEuPathDB; HostDB:ENSMFAG00000004061; -. DR GeneTree; ENSGT00950000183134; -. DR Proteomes; UP000233100; Chromosome 18. DR Bgee; ENSMFAG00000004061; Expressed in heart and 13 other cell types or tissues. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:TreeGrafter. DR GO; GO:0006090; P:pyruvate metabolic process; IEA:TreeGrafter. 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:SF27; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000106-3}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003426}; KW Reference proteome {ECO:0000313|Proteomes:UP000233100}. FT DOMAIN 52..233 FT /note="Malic enzyme N-terminal" FT /evidence="ECO:0000259|SMART:SM01274" FT DOMAIN 243..498 FT /note="Malic enzyme NAD-binding" FT /evidence="ECO:0000259|SMART:SM00919" FT ACT_SITE 75 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1" FT BINDING 128 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2" FT BINDING 218 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT BINDING 219 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT BINDING 242 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT BINDING 384 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2" FT BINDING 429 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2" SQ SEQUENCE 547 AA; 61222 MW; 5DA13EB4EF2A0B83 CRC64; MAFTLQERQM LGLQGLLPPK IETQDIQALR FHRNLKKMTS PLEKYIYIMG IQERNEKLFY RILQDDIESL MPIVYTPTVG LACSQYGHIF RRPKGLFISI SDRGHVRSIV DNWPENHVKA VVVTDGERIL GLGDLGVYGM GIPVGKLCLY TACAGIQPDR CLPVCIDVGT DNIALLKDPF YMGLYQKRDR TQQYDDLIDE FMKAITDRYG RNTLIQFEDF GNHNAFRFLR KYREKYCTFN DDIQGTAAVA LAGLLAAQKV ISKPISEHKI LFLGAGEAAL GIANLIVMSM VENGLSEQEA QKKIWMFDKY GLLVKGRKAK IDSYQEPFTH PVPESIPDTF EDAVNILKPS TIIGVAGAGR LFTPDVIRAM ASINERPVIF ALSNPTAQAE CTAAEAYTLT EGRCLFASGS PFGPVKLTDG RVFTPGQGNN VYIFPGVALA VILCNTRHIS DSVFLEAAKA LTSQLTDEEL AQGRLYPPLA NIQEVSINIA IKVTEYLYAN KMAFRYPEPE DKAKYVKERI WRSEYDSLLP DVYEWPESAS SPPVITE //