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

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P26616 (MAO1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Protein existence	Evidence 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⁺. HAMAP-Rule MF_01619
Sequence similarities	Belongs to the malic enzymes family.
Biophysicochemical properties	Kinetic parameters: At pH 7.2. K_M=0.420 mM for L-malate (Ref.6) Ref.5 Ref.6 K_M=0.66 mM for L-malate (Ref.5) K_M=0.097 mM for NAD⁺ (Ref.6) K_M=0.0688 mM for NAD⁺ (Ref.5) K_M=2.59 mM for pyruvate (Ref.5) V_max=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.

Ontologies

Keywords
Ligand	Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from mutant phenotype PubMed 11815613. Source: EcoCyc malate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (oxaloacetate-decarboxylating) activity Inferred from direct assay PubMed 9212416. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 565

565

NAD-dependent malic enzyme HAMAP-Rule MF_01619

PRO_0000160215

Sites

Active site

104

Proton donor By similarity

Active site

175

Proton acceptor By similarity

Metal binding

246

Divalent metal cation By similarity

Metal binding

247

Divalent metal cation By similarity

Metal binding

270

Divalent metal cation By similarity

Binding site

157

NAD By similarity

Binding site

270

NAD By similarity

Binding site

418

NAD By similarity

Site

270

Important for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P26616 [UniParc].

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

565

63,197

        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' referencesShow '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. 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 277:1453-1474(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]	"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.
PIR	B64901.
RefSeq	NP_415996.2. NC_000913.2. YP_489744.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P26616.
SMR	P26616. Positions 17-536.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b1479.
Proteomic databases
PaxDb	P26616.
PRIDE	P26616.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74552; AAC74552; b1479. BAA15127; BAA15127; BAA15127.
GeneID	12931214. 946031.
KEGG	ecj:Y75_p1455. eco:b1479.
PATRIC	32118252. VBIEscCol129921_1546.
Organism-specific databases
EchoBASE	EB0941.
EcoGene	EG10948. maeA.
Phylogenomic databases
eggNOG	COG0281.
HOGENOM	HOG000042487.
KO	K00027.
OMA	HCERPIV.
ProtClustDB	PRK13529.
Enzyme and pathway databases
BioCyc	EcoCyc:MALIC-NAD-MONOMER. ECOL316407:JW5238-MONOMER. MetaCyc:MALIC-NAD-MONOMER.
SABIO-RK	P26616.
Gene expression databases
Genevestigator	P26616.
Family and domain databases
Gene3D	3.40.50.10380. 1 hit. 3.40.50.720. 1 hit.
HAMAP	MF_01619. NAD_malic_enz.
InterPro	IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD-bd. IPR001891. Malic_OxRdtase. IPR016040. NAD(P)-bd_dom. IPR023667. NAD_malic_enz_proteobac. [Graphical view]
Pfam	PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. [Graphical view]
PIRSF	PIRSF000106. ME. 1 hit.
PRINTS	PR00072. MALOXRDTASE.
SMART	SM00919. Malic_M. 1 hit. [Graphical view]
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAO1_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 112 of the entry and version 4 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

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

Entry information

Relevant documents