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P26616

- MAO1_ECOLI

UniProt

P26616 - MAO1_ECOLI

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Protein
NAD-dependent malic enzyme
Gene
maeA, sfcA, b1479, JW5238
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + NAD+ = pyruvate + CO2 + NADH.UniRule annotation
Oxaloacetate = pyruvate + CO2.UniRule annotation

Cofactori

Divalent metal cations. Prefers magnesium or manganese.1 Publication

Enzyme regulationi

Non-competitively inhibited by high concentrations of NAD+ and L-malate. Also inhibited by CoA, acetyl-phosphate, palmitoyl-CoA, and oxaloacetate. Activated by aspartate.2 Publications

Kineticsi

At pH 7.2.

  1. KM=0.420 mM for L-malate (1 Publication)2 Publications
  2. KM=0.66 mM for L-malate (1 Publication)
  3. KM=0.097 mM for NAD+ (1 Publication)
  4. KM=0.0688 mM for NAD+ (1 Publication)
  5. KM=2.59 mM for pyruvate (1 Publication)

Vmax=125.47 µmol/min/mg enzyme (1 Publication

)

pH dependencei

Optimum pH is 7.2 to 7.5 for L-malate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton donor By similarity
Binding sitei157 – 1571NAD By similarity
Active sitei175 – 1751Proton acceptor By similarity
Metal bindingi246 – 2461Divalent metal cation By similarity
Metal bindingi247 – 2471Divalent metal cation By similarity
Metal bindingi270 – 2701Divalent metal cation By similarity
Binding sitei270 – 2701NAD By similarity
Sitei270 – 2701Important for activity By similarity
Binding sitei418 – 4181NAD By similarity

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. malate dehydrogenase (decarboxylating) (NAD+) activity Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. oxaloacetate decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. gluconeogenesis Source: EcoCyc
  2. malate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent malic enzyme (EC:1.1.1.38)
Short name:
NAD-ME
Gene namesi
Name:maeA
Synonyms:sfcA
Ordered Locus Names:b1479, JW5238
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10948. maeA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 565565NAD-dependent malic enzymeUniRule annotation
PRO_0000160215Add
BLAST

Proteomic databases

PaxDbiP26616.
PRIDEiP26616.

Expressioni

Gene expression databases

GenevestigatoriP26616.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP26616. 3 interactions.
STRINGi511145.b1479.

Structurei

3D structure databases

ProteinModelPortaliP26616.

Family & Domainsi

Sequence similaritiesi

Belongs to the malic enzymes family.

Phylogenomic databases

eggNOGiCOG0281.
HOGENOMiHOG000042487.
KOiK00027.
OMAiIQDNNET.
OrthoDBiEOG6QVRGM.
PhylomeDBiP26616.

Family and domain databases

Gene3Di3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01619. NAD_malic_enz.
InterProiIPR015884. 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]
PfamiPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view]
PIRSFiPIRSF000106. ME. 1 hit.
PRINTSiPR00072. MALOXRDTASE.
SMARTiSM00919. Malic_M. 1 hit.
[Graphical view]
PROSITEiPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26616-1 [UniParc]FASTAAdd to Basket

« Hide

MEPKTKKQRS LYIPYAGPVL LEFPLLNKGS AFSMEERRNF NLLGLLPEVV    50
ETIEEQAERA WIQYQGFKTE IDKHIYLRNI QDTNETLFYR LVNNHLDEMM 100
PVIYTPTVGA ACERFSEIYR RSRGVFISYQ NRHNMDDILQ NVPNHNIKVI 150
VVTDGERILG LGDQGIGGMG IPIGKLSLYT ACGGISPAYT LPVVLDVGTN 200
NQQLLNDPLY MGWRNPRITD DEYYEFVDEF IQAVKQRWPD VLLQFEDFAQ 250
KNAMPLLNRY RNEICSFNDD IQGTAAVTVG TLIAASRAAG GQLSEKKIVF 300
LGAGSAGCGI AEMIISQTQR EGLSEEAARQ KVFMVDRFGL LTDKMPNLLP 350
FQTKLVQKRE NLSDWDTDSD VLSLLDVVRN VKPDILIGVS GQTGLFTEEI 400
IREMHKHCPR PIVMPLSNPT SRVEATPQDI IAWTEGNALV ATGSPFNPVV 450
WKDKIYPIAQ CNNAFIFPGI GLGVIASGAS RITDEMLMSA SETLAQYSPL 500
VLNGEGMVLP ELKDIQKVSR AIAFAVGKMA QQQGVAVKTS AEALQQAIDD 550
NFWQAEYRDY RRTSI 565
Length:565
Mass (Da):63,197
Last modified:December 6, 2005 - v4
Checksum:iFFD61212F709EE3A
GO

Sequence cautioni

The sequence CAA39419.1 differs from that shown. Reason: The sequence differs from position 433 onward for unknown reasons.
The sequence CAA39419.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC74552.2.
AP009048 Genomic DNA. Translation: BAA15127.2.
X55956 Genomic DNA. Translation: CAA39419.1. Sequence problems.
PIRiB64901.
RefSeqiNP_415996.2. NC_000913.3.
YP_489744.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74552; AAC74552; b1479.
BAA15127; BAA15127; BAA15127.
GeneIDi12931214.
946031.
KEGGiecj:Y75_p1455.
eco:b1479.
PATRICi32118252. VBIEscCol129921_1546.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC74552.2 .
AP009048 Genomic DNA. Translation: BAA15127.2 .
X55956 Genomic DNA. Translation: CAA39419.1 . Sequence problems.
PIRi B64901.
RefSeqi NP_415996.2. NC_000913.3.
YP_489744.1. NC_007779.1.

3D structure databases

ProteinModelPortali P26616.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P26616. 3 interactions.
STRINGi 511145.b1479.

Proteomic databases

PaxDbi P26616.
PRIDEi P26616.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74552 ; AAC74552 ; b1479 .
BAA15127 ; BAA15127 ; BAA15127 .
GeneIDi 12931214.
946031.
KEGGi ecj:Y75_p1455.
eco:b1479.
PATRICi 32118252. VBIEscCol129921_1546.

Organism-specific databases

EchoBASEi EB0941.
EcoGenei EG10948. maeA.

Phylogenomic databases

eggNOGi COG0281.
HOGENOMi HOG000042487.
KOi K00027.
OMAi IQDNNET.
OrthoDBi EOG6QVRGM.
PhylomeDBi P26616.

Enzyme and pathway databases

BioCyci EcoCyc:MALIC-NAD-MONOMER.
ECOL316407:JW5238-MONOMER.
MetaCyc:MALIC-NAD-MONOMER.
SABIO-RK P26616.

Miscellaneous databases

PROi P26616.

Gene expression databases

Genevestigatori P26616.

Family and domain databases

Gene3Di 3.40.50.10380. 1 hit.
3.40.50.720. 1 hit.
HAMAPi MF_01619. NAD_malic_enz.
InterProi IPR015884. 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 ]
Pfami PF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view ]
PIRSFi PIRSF000106. ME. 1 hit.
PRINTSi PR00072. MALOXRDTASE.
SMARTi SM00919. Malic_M. 1 hit.
[Graphical view ]
PROSITEi PS00331. MALIC_ENZYMES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. "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.

Entry informationi

Entry nameiMAO1_ECOLI
AccessioniPrimary (citable) accession number: P26616
Secondary accession number(s): P78224
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, 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

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