MAOX_POPTR
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 03-AUG-2022, entry version 122.
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(+) = CO2 + NADPH + pyruvate;
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=H(+) + oxaloacetate = CO2 + pyruvate; 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}.
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DR EMBL; X56233; CAA39690.1; -; mRNA.
DR PIR; S18826; S18826.
DR AlphaFoldDB; P34105; -.
DR SMR; P34105; -.
DR STRING; 3694.POPTR_0018s09380.1; -.
DR PRIDE; P34105; -.
DR eggNOG; KOG1257; Eukaryota.
DR ExpressionAtlas; P34105; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR046346; Aminiacid_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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
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 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
