MAOX_PHAVU
ID MAOX_PHAVU Reviewed; 589 AA.
AC P12628;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=NADP-dependent malic enzyme;
DE Short=NADP-ME;
DE EC=1.1.1.40;
GN Name=ME1;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3041415; DOI=10.1073/pnas.85.15.5546;
RA Walter M.H., Grima-Pettenati J., Grand C., Boudet A.M., Lamb C.J.;
RT "Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin
RT synthesis: cDNA cloning and mRNA induction by fungal elicitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5546-5550(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Processor; TISSUE=Leaf;
RX PubMed=7925425; DOI=10.1111/j.1432-1033.1994.t01-1-00999.x;
RA Walter M.H., Grima-Pettenati J., Feuillet C.;
RT "Characterization of a bean (Phaseolus vulgaris L.) malic-enzyme gene.";
RL Eur. J. Biochem. 224:999-1009(1994).
RN [3]
RP SIMILARITY TO MALIC ENZYMES.
RX PubMed=2103472; DOI=10.1007/bf00019173;
RA Walter M.H., Grima-Pettenati J., Grand C., Boudet A.M., Lamb C.J.;
RT "Extensive sequence similarity of the bean CAD4 (cinnamyl-alcohol
RT dehydrogenase) to a maize malic enzyme.";
RL Plant Mol. Biol. 15:525-526(1990).
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 -!- INDUCTION: By fungal elicitor.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a cinnamyl-alcohol dehydrogenase.
CC {ECO:0000305|PubMed:3041415}.
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DR EMBL; J03825; AAA19575.1; -; mRNA.
DR EMBL; X80051; CAA56354.1; -; Genomic_DNA.
DR PIR; S48198; DEFBC.
DR AlphaFoldDB; P12628; -.
DR SMR; P12628; -.
DR STRING; 3885.XP_007137243.1; -.
DR PRIDE; P12628; -.
DR ProMEX; P12628; -.
DR eggNOG; KOG1257; Eukaryota.
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..589
FT /note="NADP-dependent malic enzyme"
FT /id="PRO_0000160201"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 333..349
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 304
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="K -> N (in Ref. 2; CAA56354)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> E (in Ref. 2; CAA56354)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..259
FT /note="TF -> EL (in Ref. 2; CAA56354)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="V -> L (in Ref. 2; CAA56354)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="K -> P (in Ref. 2; CAA56354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 64932 MW; 9BFADDB2699BAC1E CRC64;
MSSISLKENG GEVSVKKDYS NGGGVRDLYG EDSATEDHLI TPWTFSVASG CSLLRDPRYN
KGLAFTEGER DAHYLRGLLP PSVFNQELQE KRLMHNLRQY EVPLHRYMAL MDLQERNERL
FYKLLIDNVA ELLPVVYTPT VGEACQKYGS IFRRPQGLYI SLKEKGKILE VLKNWPEKSI
QVIVVTDGER ILGLGDLGCQ GMGIPVGKLS LYTALGGVRP SSCLPVTIDV GTNNEKLLND
EFYIGLRQRR ATGQEYATFL DEFMRAVKQN YGEKVLVQFE DFANHNAFDL LEKYSSSHLV
FNDDIQGTAS VVLAGLLASL KLVGGTLADH TFLFLGAGEA GTGIAELIAV EVSKQTKAPV
EETRKKIWLV DSKGLIVSSR LESLQQFKKP WAHEHEPVKG LLEAVKAIKP TVLIGSSGAG
KTFTKEVVET MASLNEKPLI LALSNPTSQS ECTAEEAYTW SKGRAIFASG SPFDPVEYEG
KLFVPGQANN AYIFPGFGLG LIMSGAIRVR DEMLLAASEA LAAQVSEENY DKGLIYPPFT
NIRKISANIA AKVAAKAYDL GLASHLKRPK DLVKYAESCM YSPGYRSYR