Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 175 (07 Oct 2020)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

NADP-dependent malic enzyme

Gene

maeB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Cannot use NAD+.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent metal cations. Prefers magnesium or manganese.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei94Proton acceptorBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi136Divalent metal cationBy similarity1
    Metal bindingi137Divalent metal cationBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei162NADBy similarity1
    Binding sitei288NADBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi76 – 83NADPBy similarity8

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionMultifunctional enzyme, Oxidoreductase
    LigandMetal-binding, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:MALIC-NADP-MONOMER
    MetaCyc:MALIC-NADP-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.40, 2026

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    NADP-dependent malic enzyme (EC:1.1.1.40)
    Short name:
    NADP-ME
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:maeB
    Synonyms:ypfF
    Ordered Locus Names:b2463, JW2447
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1687685

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001602421 – 759NADP-dependent malic enzymeAdd BLAST759

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei56N6-acetyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P76558

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P76558

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P76558

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P76558

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homooligomer, possibly an octamer.

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4260925, 8 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10141N

    Protein interaction database and analysis system

    More...
    IntActi
    P76558, 10 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2463

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P76558

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P76558

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 428Malic enzymeAdd BLAST428
    Regioni429 – 759Phosphate acetyltransferase; required for oligomerization, inhibition by acetyl-CoA and activation by glutamate, aspartate, and glucose-6-phosphateAdd BLAST331

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0280, Bacteria
    COG0281, Bacteria

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P76558

    KEGG Orthology (KO)

    More...
    KOi
    K00029

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P76558

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.10380, 1 hit
    3.40.50.10750, 1 hit
    3.40.50.10950, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR015884, Malic_enzyme_CS
    IPR012301, Malic_N_dom
    IPR037062, Malic_N_dom_sf
    IPR012302, Malic_NAD-bd
    IPR012188, ME_PTA
    IPR036291, NAD(P)-bd_dom_sf
    IPR042113, P_AcTrfase_dom1
    IPR042112, P_AcTrfase_dom2
    IPR002505, PTA_PTB

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00390, malic, 1 hit
    PF03949, Malic_M, 1 hit
    PF01515, PTA_PTB, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF036684, ME_PTA, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01274, malic, 1 hit
    SM00919, Malic_M, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735, SSF51735, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00331, MALIC_ENZYMES, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9A8B67D9635E25BA
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC75516.1
    AP009048 Genomic DNA Translation: BAA16337.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F65021

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416958.1, NC_000913.3
    WP_000342644.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75516; AAC75516; b2463
    BAA16337; BAA16337; BAA16337

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946947

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2447
    eco:b2463

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4277

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC75516.1
    AP009048 Genomic DNA Translation: BAA16337.1
    PIRiF65021
    RefSeqiNP_416958.1, NC_000913.3
    WP_000342644.1, NZ_LN832404.1

    3D structure databases

    SMRiP76558
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi4260925, 8 interactors
    DIPiDIP-10141N
    IntActiP76558, 10 interactors
    STRINGi511145.b2463

    Chemistry databases

    BindingDBiP76558
    ChEMBLiCHEMBL1687685

    PTM databases

    iPTMnetiP76558

    Proteomic databases

    jPOSTiP76558
    PaxDbiP76558
    PRIDEiP76558

    Genome annotation databases

    EnsemblBacteriaiAAC75516; AAC75516; b2463
    BAA16337; BAA16337; BAA16337
    GeneIDi946947
    KEGGiecj:JW2447
    eco:b2463
    PATRICifig|1411691.4.peg.4277

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB3945

    Phylogenomic databases

    eggNOGiCOG0280, Bacteria
    COG0281, Bacteria
    InParanoidiP76558
    KOiK00029
    PhylomeDBiP76558

    Enzyme and pathway databases

    BioCyciEcoCyc:MALIC-NADP-MONOMER
    MetaCyc:MALIC-NADP-MONOMER
    BRENDAi1.1.1.40, 2026

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P76558

    Family and domain databases

    Gene3Di3.40.50.10380, 1 hit
    3.40.50.10750, 1 hit
    3.40.50.10950, 1 hit
    InterProiView protein in InterPro
    IPR015884, Malic_enzyme_CS
    IPR012301, Malic_N_dom
    IPR037062, Malic_N_dom_sf
    IPR012302, Malic_NAD-bd
    IPR012188, ME_PTA
    IPR036291, NAD(P)-bd_dom_sf
    IPR042113, P_AcTrfase_dom1
    IPR042112, P_AcTrfase_dom2
    IPR002505, PTA_PTB
    PfamiView protein in Pfam
    PF00390, malic, 1 hit
    PF03949, Malic_M, 1 hit
    PF01515, PTA_PTB, 1 hit
    PIRSFiPIRSF036684, ME_PTA, 1 hit
    SMARTiView protein in SMART
    SM01274, malic, 1 hit
    SM00919, Malic_M, 1 hit
    SUPFAMiSSF51735, SSF51735, 1 hit
    PROSITEiView protein in PROSITE
    PS00331, MALIC_ENZYMES, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMAO2_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P76558
    Secondary accession number(s): P78200, P78201
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 1, 1997
    Last modified: October 7, 2020
    This is version 175 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again