NADP-dependent malic enzyme - Escherichia coli (strain K12)

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P76558 (MAO2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
NADP-dependent malic enzyme
Short name=NADP-ME
EC=1.1.1.40

Gene names

Name:	maeB
Synonyms:	ypfF
Ordered Locus Names:	b2463, JW2447

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	759 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-malate + NADP⁺ = pyruvate + CO₂ + NADPH. Oxaloacetate = pyruvate + CO₂.
Cofactor	Divalent metal cations. Prefers magnesium or manganese. Ref.5
Enzyme regulation	Inhibited by 4 mM Mg²⁺ and acetyl-CoA, competitively inhibited by fumarate and oxaloacetate. Activated by glutamate and aspartate, glucose-6-phosphate, acetyl-phosphate and 2 mM KCl. Ref.5
Subunit structure	Homooligomer, possibly an octamer.
Domain	The-C-terminal phosphate acetyltransferase domain is responsible for oligomerization, and is responsible for inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphate as shown by its deletion. The isolated domain does not catalyze the interconversion of acetyl-CoA and acetyl-phosphate. Ref.5
Miscellaneous	Cannot use NAD⁺.
Sequence similarities	In the N-terminal section; belongs to the malic enzymes family. In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.
Biophysicochemical properties	Kinetic parameters: K_M=3.41 mM for L-malate Ref.5 K_M=0.0415 mM for NADP K_M=6.21 mM for pyruvate pH dependence: Optimum pH is 7.5 for L-malate.

Ontologies

Keywords
Ligand	Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	malate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) activity Inferred from direct assay Ref.5. Source: EcoCyc manganese ion binding Inferred from direct assay PubMed 4385340. Source: EcoCyc transferase activity, transferring acyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-545413,EBI-548960

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 759

759

NADP-dependent malic enzyme

PRO_0000160242

Regions

Nucleotide binding

76 – 83

NADP By similarity

Region

1 – 428

428

Malic enzyme

Region

429 – 759

331

Phosphate acetyltransferase; required for oligomerization, inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphate

Sites

Active site

Proton acceptor By similarity

Metal binding

136

Divalent metal cation By similarity

Metal binding

137

Divalent metal cation By similarity

Binding site

162

NAD By similarity

Binding site

288

NAD By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P76558 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 9A8B67D9635E25BA
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FASTA

759

82,417

        10         20         30         40         50         60 
MDDQLKQSAL DFHEFPVPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI EKDPLKAYKY 

        70         80         90        100        110        120 
TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGIDVFDIE VDELDPDKFI 

       130        140        150        160        170        180 
EVVAALEPTF GGINLEDIKA PECFYIEQKL RERMNIPVFH DDQHGTAIIS TAAILNGLRV 

       190        200        210        220        230        240 
VEKNISDVRM VVSGAGAAAI ACMNLLVALG LQKHNIVVCD SKGVIYQGRE PNMAETKAAY 

       250        260        270        280        290        300 
AVVDDGKRTL DDVIEGADIF LGCSGPKVLT QEMVKKMARA PMILALANPE PEILPPLAKE 

       310        320        330        340        350        360 
VRPDAIICTG RSDYPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVRA IAELAHAEQS 

       370        380        390        400        410        420 
EVVASAYGDQ DLSFGPEYII PKPFDPRLIV KIAPAVAKAA MESGVATRPI ADFDVYIDKL 

       430        440        450        460        470        480 
TEFVYKTNLF MKPIFSQARK APKRVVLPEG EEARVLHATQ ELVTLGLAKP ILIGRPNVIE 

       490        500        510        520        530        540 
MRIQKLGLQI KAGVDFEIVN NESDPRFKEY WTEYFQIMKR RGVTQEQAQR ALISNPTVIG 

       550        560        570        580        590        600 
AIMVQRGEAD AMICGTVGDY HEHFSVVKNV FGYRDGVHTA GAMNALLLPS GNTFIADTYV 

       610        620        630        640        650        660 
NDEPDAEELA EITLMAAETV RRFGIEPRVA LLSHSNFGSS DCPSSSKMRQ ALELVRERAP 

       670        680        690        700        710        720 
ELMIDGEMHG DAALVEAIRN DRMPDSSLKG SANILVMPNM EAARISYNLL RVSSSEGVTV 

       730        740        750 
GPVLMGVAKP VHVLTPIASV RRIVNMVALA VVEAQTQPL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Studies on regulatory functions of malic enzymes. VI. Purification and molecular properties of NADP-linked malic enzyme from Escherichia coli W." Iwakura M., Hattori J., Arita Y., Tokushige M., Katsuki H. J. Biochem. 85:1355-1365(1979) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: W / ATCC 11105 / DSM 1900.
[5]	"Escherichia coli malic enzymes: two isoforms with substantial differences in kinetic properties, metabolic regulation, and structure." Bologna F.P., Andreo C.S., Drincovich M.F. J. Bacteriol. 189:5937-5946(2007) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, DOMAIN STRUCTURE. Strain: K12.
[6]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC75516.1. AP009048 Genomic DNA. Translation: BAA16337.1.
PIR	F65021.
RefSeq	NP_416958.1. NC_000913.2. YP_490690.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P76558.
SMR	P76558. Positions 1-406, 444-754.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10141N.
IntAct	P76558. 9 interactions.
STRING	511145.b2463.
Proteomic databases
PaxDb	P76558.
PRIDE	P76558.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75516; AAC75516; b2463. BAA16337; BAA16337; BAA16337.
GeneID	12931931. 946947.
KEGG	ecj:Y75_p2415. eco:b2463.
PATRIC	32120309. VBIEscCol129921_2557.
Organism-specific databases
EchoBASE	EB3945.
EcoGene	EG14193. maeB.
Phylogenomic databases
eggNOG	COG0281.
HOGENOM	HOG000132448.
KO	K00029.
OMA	NPDPEIG.
ProtClustDB	PRK07232.
Enzyme and pathway databases
BioCyc	EcoCyc:MALIC-NADP-MONOMER. ECOL316407:JW2447-MONOMER. MetaCyc:MALIC-NADP-MONOMER.
Gene expression databases
Genevestigator	P76558.
Family and domain databases
Gene3D	3.40.50.10380. 1 hit. 3.40.50.720. 1 hit.
InterPro	IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD-bd. IPR012188. ME_PTA. IPR016040. NAD(P)-bd_dom. IPR002505. PTA_PTB. [Graphical view]
Pfam	PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. PF01515. PTA_PTB. 1 hit. [Graphical view]
PIRSF	PIRSF036684. ME_PTA. 1 hit.
SMART	SM00919. Malic_M. 1 hit. [Graphical view]
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P76558.
ChEMBL	CHEMBL1687685.

Entry information

Entry name

MAO2_ECOLI

Accession

Primary (citable) accession number: P76558
Secondary accession number(s): P78200, P78201

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents