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UniProtKB/Swiss-Prot entry Q99KE1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MAOM_MOUSE
Primary accession number Q99KE1
Secondary accession number Q3TBM8
Integrated into Swiss-Prot on November 9, 2004
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    September 23, 2008 (Entry version 59)
Name and origin of the protein
Protein name NAD-dependent malic enzyme, mitochondrial [Precursor]
Synonyms NAD-ME
EC 1.1.1.38
Malic enzyme 2
Gene name
Name: Me2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Spleen, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK042289; BAC31216.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK050933; BAC34467.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK050980; BAC34483.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK156403; BAE33701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK171157; BAE42281.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004709; AAH04709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_663469.1; -.
UniGene Mm.36817
3D structure databases
HSSP P23368; 1GZ3. [HSSP ENTRY / PDB]
SMR Q99KE1; 21-573.
ModBase Q99KE1.
2D gel databases
REPRODUCTION-2DPAGE Q99KE1; -.
Organism-specific databases
MGI MGI:2147351; Me2.
Gene expression databases
ArrayExpress Q99KE1; -.
CleanEx MM_ME2; -.
GermOnline ENSMUSG00000024556; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR015884; Malic_enzyme_CS.
IPR012301; Malic_N.
IPR012302; Malic_NAD_bd.
IPR001891; Malic_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00390; malic; 1.
PF03949; Malic_M; 1.
Pfam graphical view of domain structure.
PRINTS PR00072; MALOXRDTASE.
PROSITE PS00331; MALIC_ENZYMES; 1.
BLOCKS Q99KE1.
Genome annotation databases
Ensembl ENSMUSG00000024556; Mus musculus. [Contig view]
GeneID 107029; -.
KEGG mmu:107029; -.
Phylogenomic databases
HOGENOM Q99KE1; -.
HOVERGEN Q99KE1; -.
Other
SOURCE Me2; Mus musculus.
ProtoNet Q99KE1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allosteric enzyme; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    18  18     Mitochondrion (By similarity). 
CHAIN   19   589  571     NAD-dependent malic enzyme, mitochondrial. PRO_0000018538
NP_BIND   311   328  18     NAD (By similarity). 
ACT_SITE   112   112        Proton donor (By similarity). 
ACT_SITE   183   183        Proton acceptor (By similarity). 
METAL   255   255        Divalent metal cation (By similarity). 
METAL   256   256        Divalent metal cation (By similarity). 
METAL   279   279        Divalent metal cation (By similarity). 
BINDING   165   165        NAD (By similarity). 
BINDING   279   279        NAD (By similarity). 
BINDING   421   421        NAD (By similarity). 
SITE   279   279  1     Important for activity (By similarity). 
Sequence information
Length: 589 AA [This is the length of the unprocessed precursor] Molecular weight: 65799 Da [This is the MW of the unprocessed precursor] CRC64: CD77AD5744B08CAB [This is a checksum on the sequence]
        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 

Q99KE1 in FASTA format

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