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Protein

NAD-dependent malic enzyme 2, mitochondrial

Gene

NAD-ME2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the regulation of sugars and amino acids metabolisms during the night period.1 Publication

Catalytic activityi

(S)-malate + NAD+ = pyruvate + CO2 + NADH.2 Publications

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Divalent metal cations. Prefers magnesium or manganese.By similarity

Enzyme regulationi

Activated by 2-ketoglutarate, phosphoenolpyruvate (PEP), fructose 1,6-biphosphate (FBP) and coenzyme A (acetyl-CoA and CoA) as homodimer and by oxaloacetate (OAA), 2-ketoglutarate, succinate, fumarate and CoA as heterodimer NAD-MEH. Repressed by succinate and fumarate as homodimer, in the presence of NAD+ and competitively toward the substrate L-malate.3 Publications

Kineticsi

kcat is 44.1 sec(-1) for the homodimer and 39 sec(-1) for the NAD-MEH heterodimer with NAD as substrate. In the presence of coenzyme A (CoA), kcat is 69.1 sec(-1) for the homodimer and 40.6 sec(-1) for the NAD-MEH heterodimer with NAD as substrate.

  1. KM=0.5 mM for NAD (homodimer)3 Publications
  2. KM=0.55 mM for NAD (NAD-MEH heterodimer)3 Publications
  3. KM=3 mM for L-malate (homodimer)3 Publications
  4. KM=2.7 mM for L-malate (NAD-MEH heterodimer)3 Publications
  5. KM=0.2 mM for L-malate (homodimer in the presence of coenzyme A (CoA))3 Publications
  6. KM=0.8 mM for L-malate (NAD-MEH heterodimer in the presence of coenzyme A (CoA))3 Publications

    pH dependencei

    Optimum pH is 6.6 for homodimer and 6.5 for NAD-MEH heterodimer. In the presence of coenzyme A (CoA), optimum pH is 6.8 for both homodimer and NAD-MEH heterodimer.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei136 – 1361Proton donorBy similarity
    Binding sitei189 – 1891NADBy similarity
    Active sitei207 – 2071Proton acceptorBy similarity
    Metal bindingi278 – 2781Divalent metal cationBy similarity
    Metal bindingi279 – 2791Divalent metal cationBy similarity
    Metal bindingi302 – 3021Divalent metal cationBy similarity
    Binding sitei302 – 3021NADBy similarity
    Sitei302 – 3021Important for activityBy similarity
    Binding sitei449 – 4491NADBy similarity

    GO - Molecular functioni

    • ATP binding Source: TAIR
    • cobalt ion binding Source: TAIR
    • malate dehydrogenase (decarboxylating) (NAD+) activity Source: TAIR
    • NAD binding Source: InterPro
    • protein homodimerization activity Source: TAIR
    • zinc ion binding Source: TAIR

    GO - Biological processi

    • malate metabolic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciARA:AT4G00570-MONOMER.
    BRENDAi1.1.1.39. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD-dependent malic enzyme 2, mitochondrial (EC:1.1.1.39)
    Short name:
    AtNAD-ME2
    Short name:
    NAD-malic enzyme 2
    Gene namesi
    Name:NAD-ME2
    Ordered Locus Names:At4g00570
    ORF Names:F6N23.16
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G00570.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • mitochondrion Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Disruption phenotypei

    When associated with NAD-ME1 disruption, loss of NAD-dependent malic enzyme activity associated with an altered steady-state levels of sugars and amino acids at the end of the light period.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3232MitochondrionSequence analysisAdd
    BLAST
    Chaini33 – 607575NAD-dependent malic enzyme 2, mitochondrialPRO_0000420148Add
    BLAST

    Proteomic databases

    PaxDbiQ8L7K9.
    PRIDEiQ8L7K9.

    Expressioni

    Tissue specificityi

    Expressed in leaves, stems, flowers, and roots (at protein level). Present in pollen.2 Publications

    Developmental stagei

    In flowers, mostly present in anthers, stigmatic papillae, gynoecium (apical part) and filaments, and, barely in sepals (at protein level). In developing siliques, localized in the apical part and the abscission zone. In seedlings, expressed in cotyledons, hypocotyls, and root tip. Accumulates slowly in leaves as they mature, in the mesophyll and the cells that surround the vascular bundles.2 Publications

    Inductioni

    Accumulates during the night period (at protein level).1 Publication

    Gene expression databases

    GenevisibleiQ8L7K9. AT.

    Interactioni

    Subunit structurei

    Homodimer. Heterodimer of two related subunits in NAD-MEH complex. Interacts with NAD-ME1.3 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: TAIR

    Protein-protein interaction databases

    BioGridi13511. 2 interactions.
    IntActiQ8L7K9. 2 interactions.
    STRINGi3702.AT4G00570.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8L7K9.
    SMRiQ8L7K9. Positions 35-604.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the malic enzymes family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG1257. Eukaryota.
    COG0281. LUCA.
    HOGENOMiHOG000042486.
    InParanoidiQ8L7K9.
    KOiK00028.
    OMAiDLAEGCC.
    OrthoDBiEOG093606EM.
    PhylomeDBiQ8L7K9.

    Family and domain databases

    Gene3Di3.40.50.10380. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR015884. Malic_enzyme_CS.
    IPR012301. Malic_N_dom.
    IPR012302. Malic_NAD-bd.
    IPR001891. Malic_OxRdtase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00390. malic. 1 hit.
    PF03949. Malic_M. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000106. ME. 1 hit.
    PRINTSiPR00072. MALOXRDTASE.
    SMARTiSM01274. malic. 1 hit.
    SM00919. Malic_M. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8L7K9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMWKNIAGLS KAAAAARTHG SRRCFSTAIP GPCIVHKRGA DILHDPWFNK
    60 70 80 90 100
    DTGFPLTERD RLGIRGLLPP RVMTCVQQCD RFIESFRSLE NNTKGEPENV
    110 120 130 140 150
    VALAKWRMLN RLHDRNETLY YRVLIDNIKD FAPIIYTPTV GLVCQNYSGL
    160 170 180 190 200
    YRRPRGMYFS AKDKGEMMSM IYNWPAPQVD MIVITDGSRI LGLGDLGVQG
    210 220 230 240 250
    IGIPIGKLDM YVAAAGINPQ RVLPIMLDVG TNNEKLLQND LYLGVRQPRL
    260 270 280 290 300
    EGEEYLEIID EFMEAAFTRW PKAVVQFEDF QAKWAFGTLE RYRKKFCMFN
    310 320 330 340 350
    DDVQGTAGVA LAGLLGTVRA QGRPISDFVN QKIVVVGAGS AGLGVTKMAV
    360 370 380 390 400
    QAVARMAGIS ESEATKNFYL IDKDGLVTTE RTKLDPGAVL FAKNPAEIRE
    410 420 430 440 450
    GASIVEVVKK VRPHVLLGLS GVGGIFNEEV LKAMRESDSC KPAIFAMSNP
    460 470 480 490 500
    TLNAECTAAD AFKHAGGNIV FASGSPFENV ELENGKVGHV NQANNMYLFP
    510 520 530 540 550
    GIGLGTLLSG ARIVTDGMLQ AASECLASYM TDEEVQKGIL YPSINNIRHI
    560 570 580 590 600
    TAEVGAAVLR AAVTDDIAEG HGDVGPKDLS HMSKEDTVNY ITRNMWFPVY

    SPLVHEK
    Length:607
    Mass (Da):66,641
    Last modified:October 1, 2002 - v1
    Checksum:i08B2D7C923B1E2B2
    GO

    Sequence cautioni

    The sequence AAC13636 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAB80866 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAB80866 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF058919 Genomic DNA. Translation: AAC13636.2. Different initiation.
    AL161472 Genomic DNA. Translation: CAB80866.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE81903.1.
    AY128396 mRNA. Translation: AAM91599.1.
    BT000075 mRNA. Translation: AAN15394.1.
    BT002046 mRNA. Translation: AAN72057.1.
    BT008375 mRNA. Translation: AAP37734.1.
    PIRiT01221.
    RefSeqiNP_191966.2. NM_116281.3.
    UniGeneiAt.34536.

    Genome annotation databases

    EnsemblPlantsiAT4G00570.1; AT4G00570.1; AT4G00570.
    GeneIDi828222.
    GrameneiAT4G00570.1; AT4G00570.1; AT4G00570.
    KEGGiath:AT4G00570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF058919 Genomic DNA. Translation: AAC13636.2. Different initiation.
    AL161472 Genomic DNA. Translation: CAB80866.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE81903.1.
    AY128396 mRNA. Translation: AAM91599.1.
    BT000075 mRNA. Translation: AAN15394.1.
    BT002046 mRNA. Translation: AAN72057.1.
    BT008375 mRNA. Translation: AAP37734.1.
    PIRiT01221.
    RefSeqiNP_191966.2. NM_116281.3.
    UniGeneiAt.34536.

    3D structure databases

    ProteinModelPortaliQ8L7K9.
    SMRiQ8L7K9. Positions 35-604.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi13511. 2 interactions.
    IntActiQ8L7K9. 2 interactions.
    STRINGi3702.AT4G00570.1.

    Proteomic databases

    PaxDbiQ8L7K9.
    PRIDEiQ8L7K9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G00570.1; AT4G00570.1; AT4G00570.
    GeneIDi828222.
    GrameneiAT4G00570.1; AT4G00570.1; AT4G00570.
    KEGGiath:AT4G00570.

    Organism-specific databases

    TAIRiAT4G00570.

    Phylogenomic databases

    eggNOGiKOG1257. Eukaryota.
    COG0281. LUCA.
    HOGENOMiHOG000042486.
    InParanoidiQ8L7K9.
    KOiK00028.
    OMAiDLAEGCC.
    OrthoDBiEOG093606EM.
    PhylomeDBiQ8L7K9.

    Enzyme and pathway databases

    BioCyciARA:AT4G00570-MONOMER.
    BRENDAi1.1.1.39. 399.

    Miscellaneous databases

    PROiQ8L7K9.

    Gene expression databases

    GenevisibleiQ8L7K9. AT.

    Family and domain databases

    Gene3Di3.40.50.10380. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR015884. Malic_enzyme_CS.
    IPR012301. Malic_N_dom.
    IPR012302. Malic_NAD-bd.
    IPR001891. Malic_OxRdtase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00390. malic. 1 hit.
    PF03949. Malic_M. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000106. ME. 1 hit.
    PRINTSiPR00072. MALOXRDTASE.
    SMARTiSM01274. malic. 1 hit.
    SM00919. Malic_M. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMAO2_ARATH
    AccessioniPrimary (citable) accession number: Q8L7K9
    Secondary accession number(s): O65266, Q9M162
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2012
    Last sequence update: October 1, 2002
    Last modified: September 7, 2016
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.