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Reviewed, UniProtKB/Swiss-Prot Q99KE1 (MAOM_MOUSE)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NAD-dependent malic enzyme, mitochondrial
      Short name=NAD-ME
    EC=1.1.1.38
Alternative name(s):
    Malic enzyme 2
Gene names
Name: Me2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

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

Cofactor

Divalent metal cations. Prefers magnesium or manganese By similarity.

Enzyme regulation

Subject to allosteric activation by fumarate By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the malic enzymes family.

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Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
NAD
   Molecular functionOxidoreductase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processmalate metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

malate dehydrogenase (oxaloacetate-decarboxylating) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1818Mitochondrion By similarity
Chain19 – 589571NAD-dependent malic enzyme, mitochondrial
PRO_0000018538

Regions

Nucleotide binding311 – 32818NAD By similarity

Sites

Active site1121Proton donor By similarity
Active site1831Proton acceptor By similarity
Metal binding2551Divalent metal cation By similarity
Metal binding2561Divalent metal cation By similarity
Metal binding2791Divalent metal cation By similarity
Binding site1651NAD By similarity
Binding site2791NAD By similarity
Binding site4211NAD By similarity
Site2791Important for activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q99KE1-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: CD77AD5744B08CAB

FASTA58965,799
        10         20         30         40         50         60 
MFSRLRAVTT PCTLTCRRVH LKEKGKPLML NPRTNKGMAF TLQERQMLGL QGLLPPKIET 

        70         80         90        100        110        120 
QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL QDDIESLMPI VYTPTVGLAC 

       130        140        150        160        170        180 
CQYGHIFRRP KGLFISISDR GHVRSIVDNW PENHVKAVVV TDGERILGLG DLGVYGMGIP 

       190        200        210        220        230        240 
VGKLCLYTAC AGIQPEKCLP VCIDVGTDNM ALLKDPFYMG LYQKRDRSQL YDDLMDEFMK 

       250        260        270        280        290        300 
AITDRYGRNT LIQFEDFGNH NAFRFLRKYQ QKYCTFNDDI QGTAAVALSG LLAAQRVINK 

       310        320        330        340        350        360 
PVSEHKILFL GAGEAALGIA NLIVLSMVES GLSEEEAQRK IWMFDKSGLL VKGRTASIDS 

       370        380        390        400        410        420 
NQEPYAHAAP ESIPATFEDA VNKLKPSVII GVAGAGPLFT HGVIKAMASI NERPIIFALS 

       430        440        450        460        470        480 
NPTAQAECTA EDAYTLTEGR CLFASGSPFE PVKLQDGRVF TPGQGNNAYI FPGVALAVIL 

       490        500        510        520        530        540 
CEARHISDTV FLEAAKALTT QLTDAELAQG RLYPSLANIQ EVSANIAIKL AEYLYANKMA 

       550        560        570        580 
FRYPEPEDKA RYVRERIWRS NYVSLLPDVY DWPESSLTPP QITEEKLPH

« Hide

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References

[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.

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Cross-references

Sequence databases

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.
IPIIPI00115977.
RefSeqNP_663469.1.
UniGeneMm.36817

3D structure databases

HSSPHSSP built from PDB template 1GZ3 based on UniProtKB P23368.
SMRQ99KE1. Positions 21-573.
ModBaseSearch...

PTM databases

PhosphoSiteQ99KE1.

2-D gel databases

REPRODUCTION-2DPAGEQ99KE1.

Proteomic databases

PRIDEQ99KE1.

Genome annotation databases

EnsemblENSMUSG00000024556. Mus musculus. [Contig view]
GeneID107029.
KEGGmmu:107029.

Organism-specific databases

MGIMGI:2147351. Me2.

Phylogenomic databases

HOGENOMQ99KE1.
HOVERGENQ99KE1.
OMAQ99KE1. QALRFHR.

Enzyme and pathway databases

BRENDA1.1.1.38. 244.

Gene expression databases

ArrayExpressQ99KE1.
BgeeQ99KE1.
CleanExMM_ME2.
GermOnlineENSMUSG00000024556. Mus musculus.

Family and domain databases

InterProIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N.
IPR012302. Malic_NAD_bd.
IPR001891. Malic_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view]
PRINTSPR00072. MALOXRDTASE.
PROSITEPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio358536.
SOURCESearch...

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Entry information

Entry nameMAOM_MOUSE
AccessionPrimary (citable) accession number: Q99KE1
Secondary accession number(s): Q3TBM8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents