MAOC_MAIZE
ID MAOC_MAIZE Reviewed; 636 AA.
AC P16243;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=NADP-dependent malic enzyme, chloroplastic {ECO:0000305};
DE Short=NADP-ME {ECO:0000303|PubMed:31235877};
DE EC=1.1.1.40 {ECO:0000269|PubMed:31235877};
DE Flags: Precursor;
GN Name=MOD1; Synonyms=ME1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73 Inbred;
RX PubMed=2584183; DOI=10.1016/s0021-9258(19)47154-8;
RA Rothermel B.A., Nelson T.;
RT "Primary structure of the maize NADP-dependent malic enzyme.";
RL J. Biol. Chem. 264:19587-19592(1989).
RN [2]
RP MUTAGENESIS OF ARG-237; ALA-387 AND ALA-392.
RX PubMed=12562758; DOI=10.1074/jbc.m212530200;
RA Detarsio E., Wheeler M.C., Campos-Bermudez V.A., Andreo C.S.,
RA Drincovich M.F.;
RT "Maize C4 NADP-malic enzyme. Expression in Escherichia coli and
RT characterization of site-directed mutants at the putative nucleoside-
RT binding sites.";
RL J. Biol. Chem. 278:13757-13764(2003).
RN [3]
RP MUTAGENESIS OF LYS-255 AND 435-LYS-LYS-436, AND 3D-STRUCTURE MODELING.
RX PubMed=15245332; DOI=10.1042/bj20040594;
RA Detarsio E., Andreo C.S., Drincovich M.F.;
RT "Basic residues play key roles in catalysis and NADP(+)-specificity in
RT maize (Zea mays L.) photosynthetic NADP(+)-dependent malic enzyme.";
RL Biochem. J. 382:1025-1030(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 62-636, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF
RP PHE-140; GLU-339; GLN-503 AND LEU-544.
RX PubMed=31235877; DOI=10.1038/s41477-019-0451-7;
RA Alvarez C.E., Bovdilova A., Hoppner A., Wolff C.C., Saigo M.,
RA Trajtenberg F., Zhang T., Buschiazzo A., Nagel-Steger L., Drincovich M.F.,
RA Lercher M.J., Maurino V.G.;
RT "Molecular adaptations of NADP-malic enzyme for its function in C4
RT photosynthesis in grasses.";
RL Nat. Plants 5:755-765(2019).
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 {ECO:0000269|PubMed:31235877}.
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 Evidence={ECO:0000269|PubMed:31235877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254;
CC Evidence={ECO:0000269|PubMed:31235877};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for malate {ECO:0000269|PubMed:31235877};
CC KM=14.9 uM for NADP {ECO:0000269|PubMed:31235877};
CC Note=kcat is 28.1 sec(-1) with malate as substrate.
CC {ECO:0000269|PubMed:31235877};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:31235877};
CC -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:31235877}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; J05130; AAA33487.1; -; mRNA.
DR PIR; A34482; DEZMMX.
DR RefSeq; NP_001105313.1; NM_001111843.1.
DR PDB; 5OU5; X-ray; 2.20 A; A/B/C/D=62-636.
DR PDBsum; 5OU5; -.
DR AlphaFoldDB; P16243; -.
DR SMR; P16243; -.
DR STRING; 4577.GRMZM2G085019_P01; -.
DR PaxDb; P16243; -.
DR PRIDE; P16243; -.
DR GeneID; 542233; -.
DR KEGG; zma:542233; -.
DR MaizeGDB; 13848; -.
DR eggNOG; KOG1257; Eukaryota.
DR OrthoDB; 435571at2759; -.
DR BRENDA; 1.1.1.40; 6752.
DR SABIO-RK; P16243; -.
DR UniPathway; UPA00322; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P16243; 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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Metal-binding; NAD; NADP; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..636
FT /note="NADP-dependent malic enzyme, chloroplastic"
FT /id="PRO_0000018547"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 380..396
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 351
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MUTAGEN 140
FT /note="F->I: Decreases kcat 8-fold. Decreases Km for NADP
FT 2-fold, increases Km for malate 2-fold."
FT /evidence="ECO:0000269|PubMed:31235877"
FT MUTAGEN 237
FT /note="R->L: Decreases kcat 530-fold. Increases Km for NADP
FT 36-fold and Km for malate 10-fold."
FT /evidence="ECO:0000269|PubMed:12562758"
FT MUTAGEN 255
FT /note="K->I: Increases Km for malate 10-fold, and Km for
FT NADP 15-fold. Decreases kcat 200-fold."
FT /evidence="ECO:0000269|PubMed:15245332"
FT MUTAGEN 339
FT /note="E->A: No effect on kcat and Km for NADP. Increases
FT Km for malate 2-fold."
FT /evidence="ECO:0000269|PubMed:31235877"
FT MUTAGEN 387
FT /note="A->G: Decreases kcat 48-fold. Increases Km for NADP
FT 4-fold. Increases Km for malate 6-fold."
FT /evidence="ECO:0000269|PubMed:12562758"
FT MUTAGEN 392
FT /note="A->G: No effect on kcat. Increases Km for NADP 3.5-
FT fold. Increases Km for malate 2.5-fold."
FT /evidence="ECO:0000269|PubMed:12562758"
FT MUTAGEN 435..436
FT /note="KK->LL: No effect on kcat and on Km for malate.
FT Increases Km for NADP 9-fold."
FT /evidence="ECO:0000269|PubMed:15245332"
FT MUTAGEN 503
FT /note="Q->E: No effect on kcat and Km for NADP. Increases
FT Km for malate 2-fold."
FT /evidence="ECO:0000269|PubMed:31235877"
FT MUTAGEN 544
FT /note="L->F: No effect on kcat and Km for NADP. Increases
FT Km for malate 2-fold."
FT /evidence="ECO:0000269|PubMed:31235877"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:5OU5"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 300..318
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:5OU5"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5OU5"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 354..370
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 386..403
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:5OU5"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 433..438
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 448..455
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 501..506
FT /evidence="ECO:0007829|PDB:5OU5"
FT TURN 507..510
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:5OU5"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 541..551
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 558..569
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 574..578
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 589..606
FT /evidence="ECO:0007829|PDB:5OU5"
FT HELIX 619..626
FT /evidence="ECO:0007829|PDB:5OU5"
SQ SEQUENCE 636 AA; 69824 MW; DF2D36FD4B2682EA CRC64;
MLSTRTAAVA ASASPASPWK LGGRSEGGAS CDGCRTYRNT LRRRAAPAKV RALPPRRVDA
VAMVSNAETE TEKEQEEAAA ASEELPVMPW ATSVASGYTL LRDPHHNKGL AFTEEERDGH
YLRGLLPPAV LSQELQIKKF MNTLRQYQTP LQRYIAMMNL QETDERLFYK LLIDNVVELL
PFVYTPTVGE ACQKYGSIFG RPQGLYVSLK DKGKVLEVLR NWPHRNIQVI CVTDGERILG
LGDLGCQGMG IPVGKLALYT ALGGVDPSVC LPITIDVGTN NEFLLNDEFY IGLRQKRATG
EEYDELIEEF MSAVKQFYGE KVLIQFEDFA NHNAFDLLEK YSKSHLVFND DIQGTASVVL
AGLLAALKMV GGTLAEQTYL FLGAGEAGTG IAELIALEIS KQTNAPIEEC RKKVWLVDSK
GLIVDSRKGS LQPFKKPWAH EHEPLKTLYD AVQSIKPTVL IGTSGVGRTF TKEIIEAMSS
FNERPIIFSL SNPTSHSECT AEQAYTWSQG RSIFASGSPF APVEYEGKTF VPGQSNNAYI
FPGLGLGLVI SGAVRVHEDM LLAASKALAD QATQDNFEKG SIFPPFTSIR KISAHIAAAV
AGKAYELGLA TRLPPPSDLV KYAENCMYTP VYRNYR
