MAO1_ARATH
ID MAO1_ARATH Reviewed; 623 AA.
AC Q9SIU0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=NAD-dependent malic enzyme 1, mitochondrial;
DE Short=AtNAD-ME1;
DE Short=NAD-malic enzyme 1;
DE EC=1.1.1.39;
DE Flags: Precursor;
GN Name=NAD-ME1; OrderedLocusNames=At2g13560; ORFNames=T10F5.10;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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, AND CATALYTIC ACTIVITY.
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 ACTIVITY REGULATION, INTERACTION WITH NAD-ME2, 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, AND MUTAGENESIS OF ARG-122.
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 oxaloacetate (OAA), 2-ketoglutarate,
CC succinate and fumarate as homodimer and by OAA, 2-ketoglutarate,
CC succinate, fumarate and coenzyme A (acetyl-CoA and CoA) as heterodimer
CC NAD-MEH. {ECO:0000269|PubMed:20133948, 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};
CC KM=0.55 mM for NAD (NAD-MEH heterodimer)
CC {ECO:0000269|PubMed:18223148, ECO:0000269|PubMed:20133948};
CC KM=3 mM for L-malate (homodimer) {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948};
CC KM=2.7 mM for L-malate (NAD-MEH heterodimer)
CC {ECO:0000269|PubMed:18223148, ECO:0000269|PubMed:20133948};
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};
CC Note=kcat is 31.1 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 40.6 sec(-1) for the NAD-MEH heterodimer
CC with NAD as substrate.;
CC pH dependence:
CC Optimum pH is 6.4 for homodimer and 6.5 for NAD-MEH heterodimer. In
CC the presence of coenzyme A (CoA), optimum pH is 6.8 for NAD-MEH
CC heterodimer. {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948};
CC -!- SUBUNIT: Homodimer. Heterodimer of two related subunits in NAD-MEH
CC complex. Interacts with NAD-ME2. {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). {ECO:0000269|PubMed:18223148,
CC ECO:0000269|PubMed:20133948}.
CC -!- DEVELOPMENTAL STAGE: In flowers, mostly present in sepals, stigmatic
CC papillae, gynoecium (apical part) and filaments. Excluded from anthers
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-ME2 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}.
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DR EMBL; AC007063; AAD22679.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06242.1; -; Genomic_DNA.
DR EMBL; AY091108; AAM14058.1; -; mRNA.
DR EMBL; BT000996; AAN41396.1; -; mRNA.
DR PIR; E84508; E84508.
DR RefSeq; NP_178980.1; NM_126936.4.
DR AlphaFoldDB; Q9SIU0; -.
DR SMR; Q9SIU0; -.
DR BioGRID; 1203; 3.
DR STRING; 3702.AT2G13560.1; -.
DR MetOSite; Q9SIU0; -.
DR PaxDb; Q9SIU0; -.
DR PRIDE; Q9SIU0; -.
DR ProteomicsDB; 238877; -.
DR EnsemblPlants; AT2G13560.1; AT2G13560.1; AT2G13560.
DR GeneID; 815842; -.
DR Gramene; AT2G13560.1; AT2G13560.1; AT2G13560.
DR KEGG; ath:AT2G13560; -.
DR Araport; AT2G13560; -.
DR TAIR; locus:2054085; AT2G13560.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; Q9SIU0; -.
DR OMA; PRCFTTA; -.
DR OrthoDB; 435571at2759; -.
DR PhylomeDB; Q9SIU0; -.
DR BioCyc; ARA:AT2G13560-MON; -.
DR BRENDA; 1.1.1.39; 399.
DR PRO; PR:Q9SIU0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIU0; baseline and differential.
DR Genevisible; Q9SIU0; AT.
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:UniProtKB.
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..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..623
FT /note="NAD-dependent malic enzyme 1, mitochondrial"
FT /id="PRO_0000420147"
FT ACT_SITE 143
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 122
FT /note="Required for fumarate-mediated allosteric
FT activation"
FT SITE 309
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MUTAGEN 122
FT /note="R->A: Impaired fumarate-mediated allosteric
FT activation."
FT /evidence="ECO:0000269|PubMed:22487558"
SQ SEQUENCE 623 AA; 69656 MW; C4A83798797E786E CRC64;
MGIANKLRLS SSSLSRILHR RILYSSAVRS FTTSEGHRPT IVHKQGLDIL HDPWFNKGTA
FTMTERNRLD LRGLLPPNVM DSEQQIFRFM TDLKRLEEQA RDGPSDPNAL AKWRILNRLH
DRNETMYYKV LINNIEEYAP IVYTPTVGLV CQNYSGLFRR PRGMYFSAED RGEMMSMVYN
WPAEQVDMIV VTDGSRILGL GDLGVHGIGI AVGKLDLYVA AAGINPQRVL PVMIDVGTNN
EKLRNDPMYL GLQQRRLEDD DYIDVIDEFM EAVYTRWPHV IVQFEDFQSK WAFKLLQRYR
CTYRMFNDDV QGTAGVAIAG LLGAVRAQGR PMIDFPKMKI VVAGAGSAGI GVLNAARKTM
ARMLGNTETA FDSAQSQFWV VDAQGLITEG RENIDPEAQP FARKTKEMER QGLKEGATLV
EVVREVKPDV LLGLSAVGGL FSKEVLEAMK GSTSTRPAIF AMSNPTKNAE CTPQDAFSIL
GENMIFASGS PFKNVEFGNG HVGHCNQGNN MYLFPGIGLG TLLSGAPIVS DGMLQAASEC
LAAYMSEEEV LEGIIYPPIS RIRDITKRIA AAVIKEAIEE DLVEGYREMD AREIQKLDEE
GLMEYVENNM WNPEYPTLVY KDD
