MAOC_SOLLC
ID MAOC_SOLLC Reviewed; 573 AA.
AC P37222;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=NADP-dependent malic enzyme, chloroplastic;
DE Short=NADP-ME;
DE EC=1.1.1.40;
DE Flags: Fragment;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Rutgers;
RA Finger F.L., Knee M., Lagrimini L.M.A.;
RT "Isolation of a cDNA clone for tomato fruit NADP+ malic enzyme.";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The chloroplastic ME isoform decarboxylates malate shuttled
CC from neighboring mesophyll cells. The CO(2) released is then refixed by
CC ribulose-bisphosphate carboxylase. This pathway eliminates the
CC photorespiratory loss of CO(2) that occurs in most plants.
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 -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; L27509; AAA34174.1; -; mRNA.
DR PIR; T07088; T07088.
DR AlphaFoldDB; P37222; -.
DR SMR; P37222; -.
DR STRING; 4081.Solyc12g044600.2.1; -.
DR PaxDb; P37222; -.
DR PRIDE; P37222; -.
DR eggNOG; KOG1257; Eukaryota.
DR UniPathway; UPA00322; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P37222; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IBA:GO_Central.
DR GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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 Chloroplast; Metal-binding; NAD; NADP; Oxidoreductase; Plastid;
KW Reference proteome.
FT CHAIN <1..573
FT /note="NADP-dependent malic enzyme, chloroplastic"
FT /id="PRO_0000160199"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 318..334
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 289
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 573 AA; 63561 MW; 13846E61206F8E75 CRC64;
IRHESTVTGG VQDVYGEDSA TEDQSITPWT LSVASGFSLL RNPHYNKGLA FSERERDTHY
LRGLLPPVVI SHDLQVKKMM NSIRKYDVPL QRYMAMMDLQ EMNERLFYKL LIDNVEELLP
IVYTPTVGEA CQKYGWIFKR PQGLFFSLKE KGKIHEVLKN WPEKKIQVIV VTDGERILGL
GDLGCQGMGI PVGKLSLYSA LGGIRPSACL PVTIDVGQTM KFVDDEFYIG LRQRRATGQE
YSELLDEFMY AVKQNYGEKV LIQFEDFANH NAFNLLAKYG TSHLVFNDDI QGTASVVLAG
LMAALNLVGG SLSEHTFLFL GAGEAGTGIA ELIALEMSKQ TGIPLEETRK KIWMVDSKGL
IVKSRMEMLQ HFKRPWAHDH EPVQELVNAV KSIKPTVLIG SSGAGRTFTK EVVQAMATFN
EKPIIFALSN PTSQSECTAE EAYSWSEGRA IFASGSPFAP VEYNGKVYAS GQANNAYIFP
GFGLGLIISG AIRVHDDMLL VASEALADEV SQENFEKGTH IPPFSNIRKI SAHIAKVAAK
AYELGLATRL PQPKDLVAYA ESCMYSPAYR SYR
