MAO2_ARATH
ID MAO2_ARATH Reviewed; 607 AA.
AC Q8L7K9; O65266; Q9M162;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=NAD-dependent malic enzyme 2, mitochondrial;
DE Short=AtNAD-ME2;
DE Short=NAD-malic enzyme 2;
DE EC=1.1.1.39;
DE Flags: Precursor;
GN Name=NAD-ME2; OrderedLocusNames=At4g00570; ORFNames=F6N23.16;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DISRUPTION PHENOTYPE, AND INDUCTION BY DARKNESS.
RX PubMed=18223148; DOI=10.1104/pp.107.114975;
RA Tronconi M.A., Fahnenstich H., Gerrard Weehler M.C., Andreo C.S.,
RA Fluegge U.-I., Drincovich M.F., Maurino V.G.;
RT "Arabidopsis NAD-malic enzyme functions as a homodimer and heterodimer and
RT has a major impact on nocturnal metabolism.";
RL Plant Physiol. 146:1540-1552(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP SUBUNIT, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=20528775; DOI=10.1042/bj20100497;
RA Tronconi M.A., Gerrard Wheeler M.C., Maurino V.G., Drincovich M.F.,
RA Andreo C.S.;
RT "NAD-malic enzymes of Arabidopsis thaliana display distinct kinetic
RT mechanisms that support differences in physiological control.";
RL Biochem. J. 430:295-303(2010).
RN [7]
RP TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE,
RP INTERACTION WITH NAD-ME1, ACTIVITY REGULATION, SUBUNIT, IDENTIFICATION IN
RP NAD-MEH COMPLEX, SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20133948; DOI=10.1074/jbc.m109.097477;
RA Tronconi M.A., Maurino V.G., Andreo C.S., Drincovich M.F.;
RT "Three different and tissue-specific NAD-malic enzymes generated by
RT alternative subunit association in Arabidopsis thaliana.";
RL J. Biol. Chem. 285:11870-11879(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=21841088; DOI=10.1104/pp.111.182352;
RA Klodmann J., Senkler M., Rode C., Braun H.-P.;
RT "Defining the protein complex proteome of plant mitochondria.";
RL Plant Physiol. 157:587-598(2011).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=22487558; DOI=10.1016/j.biochi.2012.03.017;
RA Tronconi M.A., Gerrard Wheeler M.C., Drincovich M.F., Andreo C.S.;
RT "Differential fumarate binding to Arabidopsis NAD+-malic enzymes 1 and -2
RT produces an opposite activity modulation.";
RL Biochimie 94:1421-1430(2012).
CC -!- FUNCTION: Involved in the regulation of sugars and amino acids
CC metabolisms during the night period. {ECO:0000269|PubMed:18223148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.39;
CC Evidence={ECO:0000269|PubMed:18223148, ECO:0000269|PubMed:20528775};
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 2-ketoglutarate, phosphoenolpyruvate
CC (PEP), fructose 1,6-biphosphate (FBP) and coenzyme A (acetyl-CoA and
CC CoA) as homodimer and by oxaloacetate (OAA), 2-ketoglutarate,
CC succinate, fumarate and CoA as heterodimer NAD-MEH. Repressed by
CC succinate and fumarate as homodimer, in the presence of NAD(+) and
CC competitively toward the substrate L-malate.
CC {ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:20528775,
CC ECO:0000269|PubMed:22487558}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for NAD (homodimer) {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:20528775};
CC KM=0.55 mM for NAD (NAD-MEH heterodimer)
CC {ECO:0000269|PubMed:18223148, ECO:0000269|PubMed:20133948,
CC ECO:0000269|PubMed:20528775};
CC KM=3 mM for L-malate (homodimer) {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:20528775};
CC KM=2.7 mM for L-malate (NAD-MEH heterodimer)
CC {ECO:0000269|PubMed:18223148, ECO:0000269|PubMed:20133948,
CC ECO:0000269|PubMed:20528775};
CC KM=0.2 mM for L-malate (homodimer in the presence of coenzyme A
CC (CoA)) {ECO:0000269|PubMed:18223148, ECO:0000269|PubMed:20133948,
CC ECO:0000269|PubMed:20528775};
CC KM=0.8 mM for L-malate (NAD-MEH heterodimer in the presence of
CC coenzyme A (CoA)) {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:20528775};
CC Note=kcat is 44.1 sec(-1) for the homodimer and 39 sec(-1) for the
CC NAD-MEH heterodimer with NAD as substrate. In the presence of
CC coenzyme A (CoA), kcat is 69.1 sec(-1) for the homodimer and 40.6
CC sec(-1) for the NAD-MEH heterodimer with NAD as substrate.;
CC pH dependence:
CC Optimum pH is 6.6 for homodimer and 6.5 for NAD-MEH heterodimer. In
CC the presence of coenzyme A (CoA), optimum pH is 6.8 for both
CC homodimer and NAD-MEH heterodimer. {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:20528775};
CC -!- SUBUNIT: Homodimer. Heterodimer of two related subunits in NAD-MEH
CC complex. Interacts with NAD-ME1. {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:20528775}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:20133948, ECO:0000269|PubMed:21841088}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, and roots (at
CC protein level). Present in pollen. {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948}.
CC -!- DEVELOPMENTAL STAGE: In flowers, mostly present in anthers, stigmatic
CC papillae, gynoecium (apical part) and filaments, and, barely in sepals
CC (at protein level). In developing siliques, localized in the apical
CC part and the abscission zone. In seedlings, expressed in cotyledons,
CC hypocotyls, and root tip. Accumulates slowly in leaves as they mature,
CC in the mesophyll and the cells that surround the vascular bundles.
CC {ECO:0000269|PubMed:18223148, ECO:0000269|PubMed:20133948}.
CC -!- INDUCTION: Accumulates during the night period (at protein level).
CC {ECO:0000269|PubMed:18223148}.
CC -!- DISRUPTION PHENOTYPE: When associated with NAD-ME1 disruption, loss of
CC NAD-dependent malic enzyme activity associated with an altered steady-
CC state levels of sugars and amino acids at the end of the light period.
CC {ECO:0000269|PubMed:18223148}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13636.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80866.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80866.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF058919; AAC13636.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL161472; CAB80866.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81903.1; -; Genomic_DNA.
DR EMBL; AY128396; AAM91599.1; -; mRNA.
DR EMBL; BT000075; AAN15394.1; -; mRNA.
DR EMBL; BT002046; AAN72057.1; -; mRNA.
DR EMBL; BT008375; AAP37734.1; -; mRNA.
DR PIR; T01221; T01221.
DR RefSeq; NP_191966.2; NM_116281.4.
DR AlphaFoldDB; Q8L7K9; -.
DR SMR; Q8L7K9; -.
DR BioGRID; 13511; 2.
DR IntAct; Q8L7K9; 2.
DR STRING; 3702.AT4G00570.1; -.
DR MetOSite; Q8L7K9; -.
DR PaxDb; Q8L7K9; -.
DR PRIDE; Q8L7K9; -.
DR ProteomicsDB; 250671; -.
DR EnsemblPlants; AT4G00570.1; AT4G00570.1; AT4G00570.
DR GeneID; 828222; -.
DR Gramene; AT4G00570.1; AT4G00570.1; AT4G00570.
DR KEGG; ath:AT4G00570; -.
DR Araport; AT4G00570; -.
DR TAIR; locus:2127038; AT4G00570.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; Q8L7K9; -.
DR OMA; AETWAYP; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; Q8L7K9; -.
DR BioCyc; ARA:AT4G00570-MON; -.
DR BRENDA; 1.1.1.39; 399.
DR PRO; PR:Q8L7K9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7K9; baseline and differential.
DR Genevisible; Q8L7K9; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IDA:TAIR.
DR GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006108; P:malate metabolic process; IDA:TAIR.
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 Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..607
FT /note="NAD-dependent malic enzyme 2, mitochondrial"
FT /id="PRO_0000420148"
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="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
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 302
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 302
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 607 AA; 66641 MW; 08B2D7C923B1E2B2 CRC64;
MMWKNIAGLS KAAAAARTHG SRRCFSTAIP GPCIVHKRGA DILHDPWFNK DTGFPLTERD
RLGIRGLLPP RVMTCVQQCD RFIESFRSLE NNTKGEPENV VALAKWRMLN RLHDRNETLY
YRVLIDNIKD FAPIIYTPTV GLVCQNYSGL YRRPRGMYFS AKDKGEMMSM IYNWPAPQVD
MIVITDGSRI LGLGDLGVQG IGIPIGKLDM YVAAAGINPQ RVLPIMLDVG TNNEKLLQND
LYLGVRQPRL EGEEYLEIID EFMEAAFTRW PKAVVQFEDF QAKWAFGTLE RYRKKFCMFN
DDVQGTAGVA LAGLLGTVRA QGRPISDFVN QKIVVVGAGS AGLGVTKMAV QAVARMAGIS
ESEATKNFYL IDKDGLVTTE RTKLDPGAVL FAKNPAEIRE GASIVEVVKK VRPHVLLGLS
GVGGIFNEEV LKAMRESDSC KPAIFAMSNP TLNAECTAAD AFKHAGGNIV FASGSPFENV
ELENGKVGHV NQANNMYLFP GIGLGTLLSG ARIVTDGMLQ AASECLASYM TDEEVQKGIL
YPSINNIRHI TAEVGAAVLR AAVTDDIAEG HGDVGPKDLS HMSKEDTVNY ITRNMWFPVY
SPLVHEK
