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Protein

NAD-dependent malic enzyme, mitochondrial

Gene

Me2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

Subject to allosteric activation by fumarate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei112 – 1121Proton donorBy similarity
Binding sitei165 – 1651NADBy similarity
Active sitei183 – 1831Proton acceptorBy similarity
Metal bindingi255 – 2551Divalent metal cationBy similarity
Metal bindingi256 – 2561Divalent metal cationBy similarity
Metal bindingi279 – 2791Divalent metal cationBy similarity
Binding sitei279 – 2791NADBy similarity
Sitei279 – 2791Important for activityBy similarity
Binding sitei421 – 4211NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi311 – 32818NADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD

Enzyme and pathway databases

BRENDAi1.1.1.38. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent malic enzyme, mitochondrial (EC:1.1.1.38)
Short name:
NAD-ME
Alternative name(s):
Malic enzyme 2
Gene namesi
Name:Me2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:2147351. Me2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818MitochondrionBy similarityAdd
BLAST
Chaini19 – 589571NAD-dependent malic enzyme, mitochondrialPRO_0000018538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561N6-acetyllysineBy similarity
Modified residuei224 – 2241N6-acetyllysineBy similarity
Modified residuei240 – 2401N6-acetyllysineBy similarity
Modified residuei272 – 2721N6-acetyllysineBy similarity
Modified residuei346 – 3461N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99KE1.
MaxQBiQ99KE1.
PaxDbiQ99KE1.
PeptideAtlasiQ99KE1.
PRIDEiQ99KE1.

2D gel databases

REPRODUCTION-2DPAGEQ99KE1.

PTM databases

PhosphoSiteiQ99KE1.

Expressioni

Gene expression databases

BgeeiQ99KE1.
CleanExiMM_ME2.
GenevisibleiQ99KE1. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ99KE1. 1 interaction.
MINTiMINT-4101121.
STRINGi10090.ENSMUSP00000025439.

Structurei

3D structure databases

ProteinModelPortaliQ99KE1.
SMRiQ99KE1. Positions 23-573.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the malic enzymes family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1257. Eukaryota.
COG0281. LUCA.
GeneTreeiENSGT00390000000754.
HOGENOMiHOG000042486.
HOVERGENiHBG000746.
InParanoidiQ99KE1.
KOiK00027.
OMAiEPFTHSA.
OrthoDBiEOG7G4QF0.
PhylomeDBiQ99KE1.
TreeFamiTF300537.

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.

Q99KE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSRLRAVTT PCTLTCRRVH LKEKGKPLML NPRTNKGMAF TLQERQMLGL
60 70 80 90 100
QGLLPPKIET QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL
110 120 130 140 150
QDDIESLMPI VYTPTVGLAC CQYGHIFRRP KGLFISISDR GHVRSIVDNW
160 170 180 190 200
PENHVKAVVV TDGERILGLG DLGVYGMGIP VGKLCLYTAC AGIQPEKCLP
210 220 230 240 250
VCIDVGTDNM ALLKDPFYMG LYQKRDRSQL YDDLMDEFMK AITDRYGRNT
260 270 280 290 300
LIQFEDFGNH NAFRFLRKYQ QKYCTFNDDI QGTAAVALSG LLAAQRVINK
310 320 330 340 350
PVSEHKILFL GAGEAALGIA NLIVLSMVES GLSEEEAQRK IWMFDKSGLL
360 370 380 390 400
VKGRTASIDS NQEPYAHAAP ESIPATFEDA VNKLKPSVII GVAGAGPLFT
410 420 430 440 450
HGVIKAMASI NERPIIFALS NPTAQAECTA EDAYTLTEGR CLFASGSPFE
460 470 480 490 500
PVKLQDGRVF TPGQGNNAYI FPGVALAVIL CEARHISDTV FLEAAKALTT
510 520 530 540 550
QLTDAELAQG RLYPSLANIQ EVSANIAIKL AEYLYANKMA FRYPEPEDKA
560 570 580
RYVRERIWRS NYVSLLPDVY DWPESSLTPP QITEEKLPH
Length:589
Mass (Da):65,799
Last modified:June 1, 2001 - v1
Checksum:iCD77AD5744B08CAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042289 mRNA. Translation: BAC31216.1.
AK050933 mRNA. Translation: BAC34467.1.
AK050980 mRNA. Translation: BAC34483.1.
AK156403 mRNA. Translation: BAE33701.1.
AK171157 mRNA. Translation: BAE42281.1.
BC004709 mRNA. Translation: AAH04709.1.
CCDSiCCDS29339.1.
RefSeqiNP_663469.1. NM_145494.2.
UniGeneiMm.36817.
Mm.459181.

Genome annotation databases

EnsembliENSMUST00000025439; ENSMUSP00000025439; ENSMUSG00000024556.
GeneIDi107029.
KEGGimmu:107029.
UCSCiuc008fox.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042289 mRNA. Translation: BAC31216.1.
AK050933 mRNA. Translation: BAC34467.1.
AK050980 mRNA. Translation: BAC34483.1.
AK156403 mRNA. Translation: BAE33701.1.
AK171157 mRNA. Translation: BAE42281.1.
BC004709 mRNA. Translation: AAH04709.1.
CCDSiCCDS29339.1.
RefSeqiNP_663469.1. NM_145494.2.
UniGeneiMm.36817.
Mm.459181.

3D structure databases

ProteinModelPortaliQ99KE1.
SMRiQ99KE1. Positions 23-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99KE1. 1 interaction.
MINTiMINT-4101121.
STRINGi10090.ENSMUSP00000025439.

PTM databases

PhosphoSiteiQ99KE1.

2D gel databases

REPRODUCTION-2DPAGEQ99KE1.

Proteomic databases

EPDiQ99KE1.
MaxQBiQ99KE1.
PaxDbiQ99KE1.
PeptideAtlasiQ99KE1.
PRIDEiQ99KE1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025439; ENSMUSP00000025439; ENSMUSG00000024556.
GeneIDi107029.
KEGGimmu:107029.
UCSCiuc008fox.1. mouse.

Organism-specific databases

CTDi4200.
MGIiMGI:2147351. Me2.

Phylogenomic databases

eggNOGiKOG1257. Eukaryota.
COG0281. LUCA.
GeneTreeiENSGT00390000000754.
HOGENOMiHOG000042486.
HOVERGENiHBG000746.
InParanoidiQ99KE1.
KOiK00027.
OMAiEPFTHSA.
OrthoDBiEOG7G4QF0.
PhylomeDBiQ99KE1.
TreeFamiTF300537.

Enzyme and pathway databases

BRENDAi1.1.1.38. 3474.

Miscellaneous databases

ChiTaRSiMe2. mouse.
PROiQ99KE1.
SOURCEiSearch...

Gene expression databases

BgeeiQ99KE1.
CleanExiMM_ME2.
GenevisibleiQ99KE1. MM.

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...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMAOM_MOUSE
AccessioniPrimary (citable) accession number: Q99KE1
Secondary accession number(s): Q3TBM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This isoenzyme can also use NADP+ but is more effective with NAD+.By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.