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P76558

- MAO2_ECOLI

UniProt

P76558 - MAO2_ECOLI

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Protein

NADP-dependent malic enzyme

Gene

maeB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NADP+ = pyruvate + CO2 + NADPH.
Oxaloacetate = pyruvate + CO2.

Cofactori

Divalent metal cations. Prefers magnesium or manganese.1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=3.41 mM for L-malate1 Publication
  2. KM=0.0415 mM for NADP1 Publication
  3. KM=6.21 mM for pyruvate1 Publication

pH dependencei

Optimum pH is 7.5 for L-malate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941Proton acceptorBy similarity
Metal bindingi136 – 1361Divalent metal cationBy similarity
Metal bindingi137 – 1371Divalent metal cationBy similarity
Binding sitei162 – 1621NADBy similarity
Binding sitei288 – 2881NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi76 – 838NADPBy similarity

GO - Molecular functioni

  1. malate dehydrogenase (decarboxylating) (NAD+) activity Source: InterPro
  2. malate dehydrogenase (decarboxylating) (NADP+) activity Source: EcoCyc
  3. manganese ion binding Source: EcoCyc
  4. NAD binding Source: InterPro
  5. oxaloacetate decarboxylase activity Source: UniProtKB-EC
  6. transferase activity, transferring acyl groups Source: InterPro

GO - Biological processi

  1. malate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NADP

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-dependent malic enzyme (EC:1.1.1.40)
Short name:
NADP-ME
Gene namesi
Name:maeB
Synonyms:ypfF
Ordered Locus Names:b2463, JW2447
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG14193. maeB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759NADP-dependent malic enzymePRO_0000160242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP76558.
PRIDEiP76558.

Expressioni

Gene expression databases

GenevestigatoriP76558.

Interactioni

Subunit structurei

Homooligomer, possibly an octamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
nadEP188431EBI-545413,EBI-548960

Protein-protein interaction databases

DIPiDIP-10141N.
IntActiP76558. 9 interactions.
STRINGi511145.b2463.

Structurei

3D structure databases

ProteinModelPortaliP76558.
SMRiP76558. Positions 1-406, 444-754.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 428428Malic enzymeAdd
BLAST
Regioni429 – 759331Phosphate acetyltransferase; required for oligomerization, inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphateAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

In the N-terminal section; belongs to the malic enzymes family.Curated
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.Curated

Phylogenomic databases

eggNOGiCOG0281.
HOGENOMiHOG000132448.
InParanoidiP76558.
KOiK00029.
OMAiDIMPDSP.
OrthoDBiEOG6QCD9W.
PhylomeDBiP76558.

Family and domain databases

Gene3Di3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N_dom.
IPR012302. Malic_NAD-bd.
IPR012188. ME_PTA.
IPR016040. NAD(P)-bd_dom.
IPR002505. PTA_PTB.
[Graphical view]
PfamiPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFiPIRSF036684. ME_PTA. 1 hit.
SMARTiSM00919. Malic_M. 1 hit.
[Graphical view]
PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76558-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDDQLKQSAL DFHEFPVPGK IQVSPTKPLA TQRDLALAYS PGVAAPCLEI
60 70 80 90 100
EKDPLKAYKY TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK
110 120 130 140 150
FAGIDVFDIE VDELDPDKFI EVVAALEPTF GGINLEDIKA PECFYIEQKL
160 170 180 190 200
RERMNIPVFH DDQHGTAIIS TAAILNGLRV VEKNISDVRM VVSGAGAAAI
210 220 230 240 250
ACMNLLVALG LQKHNIVVCD SKGVIYQGRE PNMAETKAAY AVVDDGKRTL
260 270 280 290 300
DDVIEGADIF LGCSGPKVLT QEMVKKMARA PMILALANPE PEILPPLAKE
310 320 330 340 350
VRPDAIICTG RSDYPNQVNN VLCFPFIFRG ALDVGATAIN EEMKLAAVRA
360 370 380 390 400
IAELAHAEQS EVVASAYGDQ DLSFGPEYII PKPFDPRLIV KIAPAVAKAA
410 420 430 440 450
MESGVATRPI ADFDVYIDKL TEFVYKTNLF MKPIFSQARK APKRVVLPEG
460 470 480 490 500
EEARVLHATQ ELVTLGLAKP ILIGRPNVIE MRIQKLGLQI KAGVDFEIVN
510 520 530 540 550
NESDPRFKEY WTEYFQIMKR RGVTQEQAQR ALISNPTVIG AIMVQRGEAD
560 570 580 590 600
AMICGTVGDY HEHFSVVKNV FGYRDGVHTA GAMNALLLPS GNTFIADTYV
610 620 630 640 650
NDEPDAEELA EITLMAAETV RRFGIEPRVA LLSHSNFGSS DCPSSSKMRQ
660 670 680 690 700
ALELVRERAP ELMIDGEMHG DAALVEAIRN DRMPDSSLKG SANILVMPNM
710 720 730 740 750
EAARISYNLL RVSSSEGVTV GPVLMGVAKP VHVLTPIASV RRIVNMVALA

VVEAQTQPL
Length:759
Mass (Da):82,417
Last modified:February 1, 1997 - v1
Checksum:i9A8B67D9635E25BA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC75516.1.
AP009048 Genomic DNA. Translation: BAA16337.1.
PIRiF65021.
RefSeqiNP_416958.1. NC_000913.3.
YP_490690.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75516; AAC75516; b2463.
BAA16337; BAA16337; BAA16337.
GeneIDi12931931.
946947.
KEGGiecj:Y75_p2415.
eco:b2463.
PATRICi32120309. VBIEscCol129921_2557.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC75516.1 .
AP009048 Genomic DNA. Translation: BAA16337.1 .
PIRi F65021.
RefSeqi NP_416958.1. NC_000913.3.
YP_490690.1. NC_007779.1.

3D structure databases

ProteinModelPortali P76558.
SMRi P76558. Positions 1-406, 444-754.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10141N.
IntActi P76558. 9 interactions.
STRINGi 511145.b2463.

Chemistry

BindingDBi P76558.
ChEMBLi CHEMBL1687685.

Proteomic databases

PaxDbi P76558.
PRIDEi P76558.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75516 ; AAC75516 ; b2463 .
BAA16337 ; BAA16337 ; BAA16337 .
GeneIDi 12931931.
946947.
KEGGi ecj:Y75_p2415.
eco:b2463.
PATRICi 32120309. VBIEscCol129921_2557.

Organism-specific databases

EchoBASEi EB3945.
EcoGenei EG14193. maeB.

Phylogenomic databases

eggNOGi COG0281.
HOGENOMi HOG000132448.
InParanoidi P76558.
KOi K00029.
OMAi DIMPDSP.
OrthoDBi EOG6QCD9W.
PhylomeDBi P76558.

Enzyme and pathway databases

BioCyci EcoCyc:MALIC-NADP-MONOMER.
ECOL316407:JW2447-MONOMER.
MetaCyc:MALIC-NADP-MONOMER.

Miscellaneous databases

PROi P76558.

Gene expression databases

Genevestigatori P76558.

Family and domain databases

Gene3Di 3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR015884. Malic_enzyme_CS.
IPR012301. Malic_N_dom.
IPR012302. Malic_NAD-bd.
IPR012188. ME_PTA.
IPR016040. NAD(P)-bd_dom.
IPR002505. PTA_PTB.
[Graphical view ]
Pfami PF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view ]
PIRSFi PIRSF036684. ME_PTA. 1 hit.
SMARTi SM00919. Malic_M. 1 hit.
[Graphical view ]
PROSITEi PS00331. MALIC_ENZYMES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiMAO2_ECOLI
AccessioniPrimary (citable) accession number: P76558
Secondary accession number(s): P78200, P78201
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Cannot use NAD+.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3