ID MAOX_POPTR Reviewed; 591 AA. AC P34105; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 3. DT 04-NOV-2026, entry version 139. DE RecName: Full=NADP-dependent malic enzyme; DE Short=NADP-ME; DE EC=1.1.1.40; OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. OS trichocarpa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus. OX NCBI_TaxID=3694; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX PubMed=16668348; DOI=10.1104/pp.96.4.1385; RA van Doorsselaere J., Villarroel R., van Montagu M., Inze D.; RT "Nucleotide sequence of a cDNA encoding malic enzyme from poplar."; RL Plant Physiol. 96:1385-1386(1991). 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 {ECO:0000305}. CC -!- TISSUE SPECIFICITY: mRNA found twofold higher in leaves and stems than CC in roots. 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; X56233; CAA39690.1; -; mRNA. DR PIR; S18826; S18826. DR SMR; P34105; -. DR eggNOG; KOG1257; Eukaryota. DR OMA; AACERPM; -. 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 PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1. DR PANTHER; PTHR23406:SF89; NADP-DEPENDENT MALIC ENZYME 1; 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 NCBIfam; NF010052; maeA; 1. DR PROSITE; PS00331; MALIC_ENZYMES; 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:UniProtKB-ARBA. DR AlphaFoldDB; P34105; -. PE 2: Evidence at transcript level; KW Cytoplasm; Metal-binding; NADP; Oxidoreductase. FT CHAIN 1..591 FT /note="NADP-dependent malic enzyme" FT /id="PRO_0000160203" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..10 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 139 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 210 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 192 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 282 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 283 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 306 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 306 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 335..351 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 447 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT SITE 306 FT /note="Important for activity" FT /evidence="ECO:0000250" SQ SEQUENCE 591 AA; 65223 MW; 18DF2433610F4F5A CRC64; MESTLKEMRD GASVLDMDPK STVGGGVEDV YGEDRATEDQ LVTPWTISVA SGYTLLRDPH HNKGLAFTEK ERDAHYLRGL LPPTTISQQL QEKKLMNTIR QYQLPLQKYT AMMELEERNE RLFYKLLIDN VEELLPVVYT PTVGEACQKY GSIFKRPQGL YISLKEKGKV LDVLKNWPQK SIQVIVVTDG ERILGLGDLG CQGIGIPVGK LSLYTALGGV RPSACLPVTI DVGTNNEQLL KDEFYIGLRQ RRATGQEYSE LLHEFMTAVK QNYGEKVLIQ FEDFANHNAF DLLAKYGTTH LVFNDDIQGT AAVVLAGLIS ALKLLGGSLA DHTFLFLGAG EAGTGIAELI ALEMSRRSKT PLEETRKKIW LTDSKGLIVS SRKESLQHFK KPWAHEHEPV KGLLEVVKAI KPIVLIGTSG VGKTFTKEVI EAMASFNEKP LILALSNPTS QSECTAQEAY TWTKGKAIFA SGSPFDPVEY EGKVFVPGQS NNAYIFPGLG LGLVISGAIR VHDDMLLAAA EALAGQIKEE YLAKGLIYPP LSNIRKISVQ IAANVAAKAY ELGLATRLPR PENLVKHAES CMYSPAYRYY R //