MAOP2_ARATH
ID MAOP2_ARATH Reviewed; 588 AA.
AC Q9LYG3; B9DHM4; B9DHW2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=NADP-dependent malic enzyme 2;
DE Short=AtNADP-ME2;
DE Short=NADP-malic enzyme 2;
DE EC=1.1.1.40;
GN Name=NADP-ME2; OrderedLocusNames=At5g11670; ORFNames=T22P22.60;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-588.
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16113210; DOI=10.1104/pp.105.065953;
RA Wheeler M.C., Tronconi M.A., Drincovich M.F., Andreo C.S., Fluegge U.-I.,
RA Maurino V.G.;
RT "A comprehensive analysis of the NADP-malic enzyme gene family of
RT Arabidopsis.";
RL Plant Physiol. 139:39-51(2005).
RN [6]
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19725876; DOI=10.1111/j.1742-4658.2009.07258.x;
RA Gerrard Wheeler M.C., Arias C.L., Maurino V.G., Andreo C.S.,
RA Drincovich M.F.;
RT "Identification of domains involved in the allosteric regulation of
RT cytosolic Arabidopsis thaliana NADP-malic enzymes.";
RL FEBS J. 276:5665-5677(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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:16113210};
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 Evidence={ECO:0000269|PubMed:16113210};
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 -!- ACTIVITY REGULATION: Activated by coenzyme A (CoA), aspartate,
CC succinate and fumarate. Repressed by oxaloacetate, glucose and ATP.
CC {ECO:0000269|PubMed:19725876}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=72.1 uM for NADP (at pH 7.5) {ECO:0000269|PubMed:16113210,
CC ECO:0000269|PubMed:19725876};
CC KM=3.33 mM for malate (at pH 7.5) {ECO:0000269|PubMed:16113210,
CC ECO:0000269|PubMed:19725876};
CC KM=0.5 mM for pyruvate (at pH 7) {ECO:0000269|PubMed:16113210,
CC ECO:0000269|PubMed:19725876};
CC Note=kcat is 324.1 sec(-1) with NADP and malate as substrates (at pH
CC 7.5). kcat is 75 sec(-1) with pyruvate as substrate (at pH 7).;
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:16113210,
CC ECO:0000269|PubMed:19725876};
CC -!- SUBUNIT: Homohexamers and homooctamers. {ECO:0000269|PubMed:16113210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19725876}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and roots.
CC Particularly present in vasculatures, trichome basal cells and
CC hydatodes. {ECO:0000269|PubMed:16113210}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, present in the embryo at the
CC globular and heart stages. Detected in the funiculus and vascular
CC tissues of the siliques. During germination, restricted to the proximal
CC part of the radicle having root hairs to later expands toward the
CC meristematic region, except for the root tip. Strongly expressed in
CC hypocotyls and cotyledons 6 days after imbibition. Present in primary
CC leaves. In developed flowers expressed in sepals and filaments. In
CC developing siliques, present at both ends, the stigmatic papillae and
CC the abscission zone. {ECO:0000269|PubMed:16113210}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; AL163814; CAB87685.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91708.1; -; Genomic_DNA.
DR EMBL; AF428407; AAL16175.1; -; mRNA.
DR EMBL; AK317577; BAH20241.1; -; mRNA.
DR EMBL; AK317669; BAH20329.1; -; mRNA.
DR PIR; T48526; T48526.
DR RefSeq; NP_196728.1; NM_121205.4.
DR AlphaFoldDB; Q9LYG3; -.
DR SMR; Q9LYG3; -.
DR BioGRID; 16317; 4.
DR IntAct; Q9LYG3; 2.
DR STRING; 3702.AT5G11670.1; -.
DR iPTMnet; Q9LYG3; -.
DR PaxDb; Q9LYG3; -.
DR PRIDE; Q9LYG3; -.
DR ProMEX; Q9LYG3; -.
DR ProteomicsDB; 250676; -.
DR EnsemblPlants; AT5G11670.1; AT5G11670.1; AT5G11670.
DR GeneID; 831039; -.
DR Gramene; AT5G11670.1; AT5G11670.1; AT5G11670.
DR KEGG; ath:AT5G11670; -.
DR Araport; AT5G11670; -.
DR TAIR; locus:2181980; AT5G11670.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; Q9LYG3; -.
DR OMA; DRYVFLI; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; Q9LYG3; -.
DR BioCyc; ARA:AT5G11670-MON; -.
DR BRENDA; 1.1.1.40; 399.
DR SABIO-RK; Q9LYG3; -.
DR PRO; PR:Q9LYG3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYG3; baseline and differential.
DR Genevisible; Q9LYG3; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; TAS:TAIR.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
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 Acetylation; Cytoplasm; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..588
FT /note="NADP-dependent malic enzyme 2"
FT /id="PRO_0000420150"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
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 303
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 332..348
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 303
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 588 AA; 64413 MW; 81FE889A6D252566 CRC64;
MGSTPTDLPG EDVADNRSGV GGGISDVYGE DSATLDQLVT PWVTSVASGY TLMRDPRYNK
GLAFTDKERD AHYLTGLLPP VILSQDVQER KVMHNLRQYT VPLQRYMALM DLQERNERLF
YKLLIDNVEE LLPVVYTPTV GEACQKYGSI FRKPQGLYIS LNEKGKILEV LKNWPQRGIQ
VIVVTDGERI LGLGDLGCQG MGIPVGKLSL YTALGGIRPS ACLPITIDVG TNNEKLLNDE
FYIGLKQRRA TGQEYAEFLH EFMCAVKQNY GEKVLVQFED FANHNAFDLL SKYSDSHLVF
NDDIQGTASV VLAGLIAAQK VLGKKLADHT FLFLGAGEAG TGIAELIALK ISKETGAPIT
ETRKKIWLVD SKGLIVSSRK ESLQHFKQPW AHEHKPVKDL IGAVNAIKPT VLIGTSGVGQ
TFTKEVVEAM ATNNEKPLIL ALSNPTSQAE CTAEQAYTWT KGRAIFGSGS PFDPVVYDGK
TYLPGQANNC YIFPGLGLGL IMSGAIRVRD DMLLAASEAL AAQVTEEHYA NGLIYPPFSN
IREISANIAA CVAAKTYDLG LASNLPRAKD LVKFAESSMY SPVYRNYR
