Reviewed, UniProtKB/Swiss-Prot Q8BMF3 (MAON_MOUSE)

Names and origin

Protein names

Recommended name:
    NADP-dependent malic enzyme, mitochondrial
      Short name=NADP-ME
    EC=1.1.1.40
Alternative name(s):
    Malic enzyme 3

Gene names

Name:

Me3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	604 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(S)-malate + NADP+ = pyruvate + CO2 + NADPH.
Cofactor	Divalent metal cations. Prefers magnesium or manganese By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the malic enzymes family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	malate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from sequence or structural similarity. Source: UniProtKB pyruvate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 604		NADP-dependent malic enzyme, mitochondrial		PRO_0000018540
Sites
	Active site	137	1	Proton donor By similarity
	Active site	208	1	Proton acceptor By similarity
	Metal binding	280	1	Divalent metal cation By similarity
	Metal binding	281	1	Divalent metal cation By similarity
	Metal binding	304	1	Divalent metal cation By similarity
	Binding site	190	1	NADP By similarity
	Binding site	304	1	NADP By similarity
	Binding site	443	1	NADP By similarity
	Site	304	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BMF3-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 14A0AC946D53EB21	FASTA	604	67,180
	10 20 30 40 50 60 MGAALGTGAR LTSVPRIACS SLRRQAPSAP AQGCHSKSGP PRPVPLKKRG YDVTRNPHLN 70 80 90 100 110 120 KGMAFTLEER LQLGIHGLIP PCFLSQDVQL LRIMRYYENQ QSDLDKYIIL MTHQDRNEKL 130 140 150 160 170 180 FYRVLTSDVE KFMPIVYTPT VGLACQHYGL TFRRPRGLFI TIHDKGHIAT MLNSWPEDNI 190 200 210 220 230 240 KAVVVTDGER ILGLGDLGCY GMGIPVGKLA LYTACGGVNP QQCLPVLLDV GTNNEELLRD 250 260 270 280 290 300 PLYIGLKHQR VRGEEYDDLL DEFMQAVTDK FGINCLIQFE DFANANAFRL LNKYRNKYCM 310 320 330 340 350 360 FNDDIQGTAS VAVAGILAAL RITKNRLSNH VFVFQGADEA AMGIAHLLVM ALEKEGIPKT 370 380 390 400 410 420 EAIKKIWMVD SKGLIVKGRS HLNHEKEMFA QDHPEVNSLE EVVRLVKPTA IIGVAAIAGA 430 440 450 460 470 480 FTEQILRDMA SFHERPIVFA LSNPTSKAEC TAEKCYRVTE GRGIFASGSP FKSVTLEDGR 490 500 510 520 530 540 TFTPGQGNNA YVFPGVALGV IAGGIRHIPD EIFLLTAEQI AQEVSEQHLS QGRLYPPLST 550 560 570 580 590 600 IRDVSLRIAV KVLDYAYKHN LASYYPEPKD KEAFVKSLIY TPDYDSFSLD TYSWPKEAMS VQKV

References

	« Hide 'large scale' referencesShow 'large scale' 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. , 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. Tissue: Olfactory bulb.
[2]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 71-92 AND 481-506, MASS SPECTROMETRY. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK032196 mRNA. Translation: BAC27751.1.
IPI	IPI00308976.
UniGene	Mm.334011
3D structure databases
HSSP	HSSP built from PDB template 1GQ2 based on UniProtKB P40927.
ModBase	Search...
Proteomic databases
PRIDE	Q8BMF3.
Genome annotation databases
Ensembl	ENSMUSG00000030621. Mus musculus. [Contig view]
KEGG	mmu:109264.
Organism-specific databases
MGI	MGI:1916679. Me3.
Phylogenomic databases
HOGENOM	Q8BMF3.
HOVERGEN	Q8BMF3.
Enzyme and pathway databases
BRENDA	1.1.1.40. 244.
Gene expression databases
ArrayExpress	Q8BMF3.
Bgee	Q8BMF3.
CleanEx	MM_ME3.
GermOnline	ENSMUSG00000030621. Mus musculus.
Family and domain databases
InterPro	IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD_bd. IPR001891. Malic_OxRdtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. [Graphical view]
PRINTS	PR00072. MALOXRDTASE.
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	361849.
SOURCE	Search...

Entry information

Entry name

MAON_MOUSE

Accession

Primary (citable) accession number: Q8BMF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)