MAOX_MESCR
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 03-AUG-2022, entry version 104.
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(+) = 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.
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: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; 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
