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P26616 (MAO1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD-dependent malic enzyme

Short name=NAD-ME
EC=1.1.1.38
Gene names
Name:maeA
Synonyms:sfcA
Ordered Locus Names:b1479, JW5238
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-malate + NAD+ = pyruvate + CO2 + NADH. HAMAP-Rule MF_01619

Oxaloacetate = pyruvate + CO2. HAMAP-Rule MF_01619

Cofactor

Divalent metal cations. Prefers magnesium or manganese. Ref.5

Enzyme regulation

Non-competitively inhibited by high concentrations of NAD+ and L-malate. Also inhibited by CoA, acetyl-phosphate, palmitoyl-CoA, and oxaloacetate. Activated by aspartate. Ref.5 Ref.6

Subunit structure

Homotetramer. Ref.5

Miscellaneous

Can also use NADP+ but is more effective with NAD+.

Sequence similarities

Belongs to the malic enzymes family.

Biophysicochemical properties

Kinetic parameters:

At pH 7.2.

KM=0.420 mM for L-malate (Ref.6) Ref.5 Ref.6

KM=0.66 mM for L-malate (Ref.5)

KM=0.097 mM for NAD+ (Ref.6)

KM=0.0688 mM for NAD+ (Ref.5)

KM=2.59 mM for pyruvate (Ref.5)

Vmax=125.47 µmol/min/mg enzyme (Ref.6)

pH dependence:

Optimum pH is 7.2 to 7.5 for L-malate.

Sequence caution

The sequence CAA39419.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA39419.1 differs from that shown. Reason: The sequence differs from position 433 onward for unknown reasons.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565NAD-dependent malic enzyme HAMAP-Rule MF_01619
PRO_0000160215

Sites

Active site1041Proton donor By similarity
Active site1751Proton acceptor By similarity
Metal binding2461Divalent metal cation By similarity
Metal binding2471Divalent metal cation By similarity
Metal binding2701Divalent metal cation By similarity
Binding site1571NAD By similarity
Binding site2701NAD By similarity
Binding site4181NAD By similarity
Site2701Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P26616 [UniParc].

Last modified December 6, 2005. Version 4.
Checksum: FFD61212F709EE3A

FASTA56563,197
        10         20         30         40         50         60 
MEPKTKKQRS LYIPYAGPVL LEFPLLNKGS AFSMEERRNF NLLGLLPEVV ETIEEQAERA 

        70         80         90        100        110        120 
WIQYQGFKTE IDKHIYLRNI QDTNETLFYR LVNNHLDEMM PVIYTPTVGA ACERFSEIYR 

       130        140        150        160        170        180 
RSRGVFISYQ NRHNMDDILQ NVPNHNIKVI VVTDGERILG LGDQGIGGMG IPIGKLSLYT 

       190        200        210        220        230        240 
ACGGISPAYT LPVVLDVGTN NQQLLNDPLY MGWRNPRITD DEYYEFVDEF IQAVKQRWPD 

       250        260        270        280        290        300 
VLLQFEDFAQ KNAMPLLNRY RNEICSFNDD IQGTAAVTVG TLIAASRAAG GQLSEKKIVF 

       310        320        330        340        350        360 
LGAGSAGCGI AEMIISQTQR EGLSEEAARQ KVFMVDRFGL LTDKMPNLLP FQTKLVQKRE 

       370        380        390        400        410        420 
NLSDWDTDSD VLSLLDVVRN VKPDILIGVS GQTGLFTEEI IREMHKHCPR PIVMPLSNPT 

       430        440        450        460        470        480 
SRVEATPQDI IAWTEGNALV ATGSPFNPVV WKDKIYPIAQ CNNAFIFPGI GLGVIASGAS 

       490        500        510        520        530        540 
RITDEMLMSA SETLAQYSPL VLNGEGMVLP ELKDIQKVSR AIAFAVGKMA QQQGVAVKTS 

       550        560 
AEALQQAIDD NFWQAEYRDY RRTSI 

« Hide

References

« Hide 'large scale' references
[1]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [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]"Physical analysis of spontaneous and mutagen-induced mutants of Escherichia coli K-12 expressing DNA exonuclease VIII activity."
Mahajan S.K., Chu C.C., Willis D.K., Templin A., Clark A.J.
Genetics 125:261-273(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-431.
Strain: K12.
[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, SUBUNIT.
Strain: K12.
[6]"Over-expression, purification, and characterization of recombinant NAD-malic enzyme from Escherichia coli K12."
Wang J., Tan H., Zhao Z.K.
Protein Expr. Purif. 53:97-103(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74552.2.
AP009048 Genomic DNA. Translation: BAA15127.2.
X55956 Genomic DNA. Translation: CAA39419.1. Sequence problems.
PIRB64901.
RefSeqNP_415996.2. NC_000913.3.
YP_489744.1. NC_007779.1.

3D structure databases

ProteinModelPortalP26616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP26616. 3 interactions.
STRING511145.b1479.

Proteomic databases

PaxDbP26616.
PRIDEP26616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74552; AAC74552; b1479.
BAA15127; BAA15127; BAA15127.
GeneID12931214.
946031.
KEGGecj:Y75_p1455.
eco:b1479.
PATRIC32118252. VBIEscCol129921_1546.

Organism-specific databases

EchoBASEEB0941.
EcoGeneEG10948. maeA.

Phylogenomic databases

eggNOGCOG0281.
HOGENOMHOG000042487.
KOK00027.
OMAIQDNNET.
OrthoDBEOG6QVRGM.
PhylomeDBP26616.

Enzyme and pathway databases

BioCycEcoCyc:MALIC-NAD-MONOMER.
ECOL316407:JW5238-MONOMER.
MetaCyc:MALIC-NAD-MONOMER.
SABIO-RKP26616.

Gene expression databases

GenevestigatorP26616.

Family and domain databases

Gene3D3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_01619. NAD_malic_enz.
InterProIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N_dom.
IPR012302. Malic_NAD-bd.
IPR001891. Malic_OxRdtase.
IPR016040. NAD(P)-bd_dom.
IPR023667. NAD_malic_enz_proteobac.
[Graphical view]
PfamPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view]
PIRSFPIRSF000106. ME. 1 hit.
PRINTSPR00072. MALOXRDTASE.
SMARTSM00919. Malic_M. 1 hit.
[Graphical view]
PROSITEPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP26616.

Entry information

Entry nameMAO1_ECOLI
AccessionPrimary (citable) accession number: P26616
Secondary accession number(s): P78224
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 120 of the entry and version 4 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