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P76558 (MAO2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence 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:

KM=3.41 mM for L-malate Ref.5

KM=0.0415 mM for NADP

KM=6.21 mM for pyruvate

pH dependence:

Optimum pH is 7.5 for L-malate.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nadEP188431EBI-545413,EBI-548960

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759NADP-dependent malic enzyme
PRO_0000160242

Regions

Nucleotide binding76 – 838NADP By similarity
Region1 – 428428Malic enzyme
Region429 – 759331Phosphate acetyltransferase; required for oligomerization, inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphate

Sites

Active site941Proton acceptor By similarity
Metal binding1361Divalent metal cation By similarity
Metal binding1371Divalent metal cation By similarity
Binding site1621NAD By similarity
Binding site2881NAD By similarity

Amino acid modifications

Modified residue561N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P76558 [UniParc].

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

FASTA75982,417
        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' 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. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., 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 277:1453-1462(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, IDENTIFICATION BY 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.
PIRF65021.
RefSeqNP_416958.1. NC_000913.3.
YP_490690.1. NC_007779.1.

3D structure databases

ProteinModelPortalP76558.
SMRP76558. Positions 1-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10141N.
IntActP76558. 9 interactions.
STRING511145.b2463.

Chemistry

BindingDBP76558.
ChEMBLCHEMBL1687685.

Proteomic databases

PaxDbP76558.
PRIDEP76558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75516; AAC75516; b2463.
BAA16337; BAA16337; BAA16337.
GeneID12931931.
946947.
KEGGecj:Y75_p2415.
eco:b2463.
PATRIC32120309. VBIEscCol129921_2557.

Organism-specific databases

EchoBASEEB3945.
EcoGeneEG14193. maeB.

Phylogenomic databases

eggNOGCOG0281.
HOGENOMHOG000132448.
KOK00029.
OMAYVNDDPT.
OrthoDBEOG6QCD9W.
ProtClustDBPRK07232.

Enzyme and pathway databases

BioCycEcoCyc:MALIC-NADP-MONOMER.
ECOL316407:JW2447-MONOMER.
MetaCyc:MALIC-NADP-MONOMER.

Gene expression databases

GenevestigatorP76558.

Family and domain databases

Gene3D3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
InterProIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N_dom.
IPR012302. Malic_NAD-bd.
IPR012188. ME_PTA.
IPR016040. NAD(P)-bd_dom.
IPR002505. PTA_PTB.
[Graphical view]
PfamPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFPIRSF036684. ME_PTA. 1 hit.
SMARTSM00919. Malic_M. 1 hit.
[Graphical view]
PROSITEPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP76558.

Entry information

Entry nameMAO2_ECOLI
AccessionPrimary (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: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

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