Reviewed, UniProtKB/Swiss-Prot P40375 (MAOX_SCHPO)

Names and origin

Protein names

Recommended name:
    NAD-dependent malic enzyme
      Short name=NAD-ME
    EC=1.1.1.38

Gene names

Name:	mae2
ORF Names:	SPCC794.12c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
Cofactor	Divalent metal cations. Prefers magnesium or manganese By similarity.
Sequence similarities	Belongs to the malic enzymes family.

Ontologies

Keywords
Ligand	Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	malate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyruvate metabolic process Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	NAD 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 565	565	NAD-dependent malic enzyme		PRO_0000160205
Sites
	Active site	103	1	Proton donor By similarity
	Active site	177	1	Proton acceptor By similarity
	Metal binding	248	1	Divalent metal cation By similarity
	Metal binding	249	1	Divalent metal cation By similarity
	Metal binding	272	1	Divalent metal cation By similarity
	Binding site	272	1	NAD By similarity
	Binding site	419	1	NAD By similarity
	Site	272	1	Important for activity By similarity
Amino acid modifications
	Modified residue	445	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	P40375-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: AF22D98E1BB72CA8	FASTA	565	62,535
	10 20 30 40 50 60 MPAGTKEQIE CPLKGVTLLN SPRYNKDTAF TPEERQKFEI SSRLPPIVET LQQQVDRCYD 70 80 90 100 110 120 QYKAIGDEPL QKNLYLSQLS VTNQTLFYAL ISQHLIEMIP IIYTPTEGDA IKQFSDIYRY 130 140 150 160 170 180 PEGCYLDIDH NDLSYIKQQL SEFGKSDSVE YIIITDSEGI LGIGDQGVGG VLISVAKGHL 190 200 210 220 230 240 MTLCAGLDPN RFLPIVLDVG TNNETHRKNH QYMGLRKDRV RGEQYDSFLD NVIKAIREVF 250 260 270 280 290 300 PEAFIHFEDF GLANAKRILD HYRPDIACFN DDIQGTGAVA LAAIIGALHV TKSPLTEQRI 310 320 330 340 350 360 MIFGAGTAGV GIANQIVAGM VTDGLSLDKA RGNLFMIDRC GLLLERHAKI ATDGQKPFLK 370 380 390 400 410 420 KDSDFKEVPS GDINLESAIA LVKPTILLGC SGQPGKFTEK AIREMSKHVE RPIIFPISNP 430 440 450 460 470 480 TTLMEAKPDQ IDKWSDGKAL IATGSPLPPL NRNGKKYVIS QCNNALLYPA LGVACVLSRC 490 500 510 520 530 540 KLLSDGMLKA ASDALATVPR SLFAADEALL PDLNNAREIS RHIVFAVLKQ AVSEGMSTVD 550 560 LPKDDAKLKE WIIEREWNPE YKPFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the malic enzyme gene (mae2) of Schizosaccharomyces pombe." Viljoen M., Subden R.E., Krizus A., van Vuuren H.J.J. Yeast 10:613-624(1994) [PubMed: 7941746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00621 Genomic DNA. Translation: AAA18985.1. CU329672 Genomic DNA. Translation: CAA19139.1.
PIR	S44330.
RefSeq	NP_587760.1.
3D structure databases
HSSP	HSSP built from PDB template 1GZ3 based on UniProtKB P23368.
ModBase	Search...
Genome annotation databases
GeneID	2539592.
KEGG	spo:SPCC794.12c.
NMPDR	fig|4896.1.peg.98.
Organism-specific databases
GeneDB_Spombe	SPCC794.12c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002119-MON.
Gene expression databases
ArrayExpress	P40375.
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]
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...

Entry information

Entry name

MAOX_SCHPO

Accession

Primary (citable) accession number: P40375

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)