ID MAOX_MESCR Reviewed; 585 AA. AC P37223; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=NADP-dependent malic enzyme; DE Short=NADP-ME; DE EC=1.1.1.40; GN Name=MOD1; OS Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Aizoaceae; Mesembryanthemum; OC Mesembryanthemum subgen. Cryophytum. OX NCBI_TaxID=3544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX PubMed=1521524; DOI=10.1111/j.1432-1033.1992.tb17181.x; RA Cushman J.C.; RT "Characterization and expression of a NADP-malic enzyme cDNA induced by RT salt stress from the facultative crassulacean acid metabolism plant, RT Mesembryanthemum crystallinum."; RL Eur. J. Biochem. 208:259-266(1992). CC -!- FUNCTION: Plays a role in CAM (crassulacean acid metabolism) CC photosynthesis. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NADP(+) = pyruvate + CO2 + NADPH; CC Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + H(+) = pyruvate + CO2; Xref=Rhea:RHEA:15641, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, CC ChEBI:CHEBI:16526; EC=1.1.1.40; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Divalent metal cations. Prefers magnesium or manganese. CC {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Leaves. CC -!- INDUCTION: By salt stress. CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}. 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 EMBL; X64434; CAA45772.1; -; mRNA. DR PIR; S43718; S43718. DR AlphaFoldDB; P37223; -. DR SMR; P37223; -. DR GO; GO:0009507; C:chloroplast; IEA:TreeGrafter. DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:RHEA. DR GO; GO:0006108; P:malate metabolic process; IEA:TreeGrafter. DR CDD; cd05312; NAD_bind_1_malic_enz; 1. DR FunFam; 3.40.50.10380:FF:000002; Malic enzyme; 1. DR FunFam; 3.40.50.720:FF:000067; Malic enzyme; 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 NCBIfam; NF010052; PRK13529.1; 1. DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1. DR PANTHER; PTHR23406:SF64; NADP-DEPENDENT MALIC ENZYME 3; 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 2: Evidence at transcript level; KW Cytoplasm; Metal-binding; NADP; Oxidoreductase; Stress response. FT CHAIN 1..585 FT /note="NADP-dependent malic enzyme" FT /id="PRO_0000160200" FT ACT_SITE 133 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 204 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 186 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 276 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 277 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 300 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 329..345 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 441 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT SITE 300 FT /note="Important for activity" FT /evidence="ECO:0000250" SQ SEQUENCE 585 AA; 64358 MW; C71675B67FB719D9 CRC64; MGGSNALNEM TNGSDGITGG VADVYGEEFA TQDQLVTPWS FSVACGHSLL RDPQHNKGLA FTEKERDAHF LRGLLPPVVL SQELQEKKFL TTLRQYQVPL QKYMAMMDLQ ERNEKLFYKL LVDHVEELLP LVYTPTVGEG CQKYGSIFRR PQGLFISLKD KGRILELLRN WPEKKIQVIV VTDGERILGL GDLGCQGMGI PVGKLSLYSA LGGVCPSACL PITLDVGTNN QKLLDDEFYI GLKQKRATGE EYAEFVQEFM SAVKQNYGEK ILVQFEDFAN HNAFELLEKY RTTHLVFNDD IQGTASVVLA GLIASLKLLG GTLADHKFLF LGAGEAGTGI AELIALEMSK KTKAPVEQMR KKIWLVDSKG LVVSSRKETL QQFKLPWAHE HEPITTLIDA VQAIKPTVLI GTSGKGKQFT KEVVEAMANI NAKPLILALS NPTSQSECTA EEAYTWSQGH AIFASGSPFD PVEYEGRTFV PGQANNAYIF PGFGLGLIMC GAIRVHDDML LAASEALASQ VTGEHFIKGL IYPPFKDIRK ISAHIAAGVA AKAYELGLAS RLPQPADLVK FAESCMYNPT YRSFR //