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UniProtKB - P77791 (MAA_ECOLI)

Entry version 151 (07 Apr 2021)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Maltose O-acetyltransferase

Gene

maa

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

Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars (PubMed:1856235). Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides (PubMed:12731863).2 Publications

<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 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

Acetylates glucose, maltose, mannose, galactose, and fructose with a decreasing relative rate of 1, 0.55, 0.20, 0.07, 0.04.1 Publication
  1. KM=62 mM for glucose1 Publication
  2. KM=90 mM for maltose1 Publication
  3. KM=71 mM for glucose1 Publication
  4. KM=42.9 mM for maltose1 Publication
  5. KM=285.5 mM for maltotriose1 Publication
  1. Vmax=0.20 mmol/min/mg enzyme with glucose as substrate1 Publication
  2. Vmax=0.11 mmol/min/mg enzyme with maltose as substrate1 Publication

pH dependencei

Optimum pH is 7.8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section 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 sitei83Acetyl-CoABy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei83Transition state stabilizerBy similarity1
<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 sitei113Proton donor/acceptorBy similarity1
Binding sitei140Acetyl-CoA; via amide nitrogenBy similarity1
Binding sitei158Acetyl-CoA; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei178Acetyl-CoA; shared with dimeric partnerBy similarity1
Binding sitei181Acetyl-CoABy similarity1

<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

  • identical protein binding Source: EcoCyc
  • maltose O-acetyltransferase activity Source: EcoCyc
  • O-acyltransferase activity Source: GO_Central
Complete GO annotation on QuickGO ...

<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 functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:MALTACETYLTRAN-MONOMER
MetaCyc:MALTACETYLTRAN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.79, 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:
Maltose O-acetyltransferase1 Publication (EC:2.3.1.792 Publications)
Short name:
MAT1 Publication
Alternative name(s):
Maltose transacetylase1 Publication
<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:maa
Synonyms:ylaD
Ordered Locus Names:b0459, JW0448
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000687292 – 183Maltose O-acetyltransferaseAdd BLAST182

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P77791

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

More...PaxDbi		P77791

PRoteomics IDEntifications database

More...PRIDEi		P77791

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P77791

<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

Homodimer.

1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261202, 4 interactors

Database of interacting proteins

More...DIPi		DIP-10140N

Protein interaction database and analysis system

More...IntActi		P77791, 16 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0459

<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

Secondary structure

1183
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P77791

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P77791

<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>Regioni163 – 164Acetyl-CoA binding; shared with dimeric partnerBy similarity2

<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

Belongs to the transferase hexapeptide repeat family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0110, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_051638_3_3_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P77791

Database for complete collections of gene phylogenies

More...PhylomeDBi		P77791

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001451, Hexapep
IPR018357, Hexapep_transf_CS
IPR024688, Mac_dom
IPR011004, Trimer_LpxA-like_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14602, Hexapep_2, 2 hits
PF12464, Mac, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01266, Mac, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51161, SSF51161, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00101, HEXAPEP_TRANSFERASES, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P77791-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTEKEKMIA GELYRSADET LSRDRLRARQ LIHRYNHSLA EEHTLRQQIL 
        60         70         80         90        100
ADLFGQVTEA YIEPTFRCDY GYNIFLGNNF FANFDCVMLD VCPIRIGDNC 
       110        120        130        140        150
MLAPGVHIYT ATHPIDPVAR NSGAELGKPV TIGNNVWIGG RAVINPGVTI 
       160        170        180 
GDNVVVASGA VVTKDVPDNV VVGGNPARII KKL
Length:183
Mass (Da):20,096
Last modified:January 23, 2007 - v3
<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:i3E4C7A4D68AA49C4
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
AJ223173 Genomic DNA Translation: CAA11147.1
U82664 Genomic DNA Translation: AAB40214.1
U00096 Genomic DNA Translation: AAC73561.1
AP009048 Genomic DNA Translation: BAE76238.1

Protein sequence database of the Protein Information Resource

More...PIRi		B64776

NCBI Reference Sequences

More...RefSeqi		NP_414992.1, NC_000913.3
WP_000102564.1, NZ_SSUW01000008.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73561; AAC73561; b0459
BAE76238; BAE76238; BAE76238

Database of genes from NCBI RefSeq genomes

More...GeneIDi		58460091
945096

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0448
eco:b0459

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1817

<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
AJ223173 Genomic DNA Translation: CAA11147.1
U82664 Genomic DNA Translation: AAB40214.1
U00096 Genomic DNA Translation: AAC73561.1
AP009048 Genomic DNA Translation: BAE76238.1
PIRiB64776
RefSeqiNP_414992.1, NC_000913.3
WP_000102564.1, NZ_SSUW01000008.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OCXX-ray2.15A/B/C2-183[»]
6AG8X-ray1.34A/C1-183[»]
SMRiP77791
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261202, 4 interactors
DIPiDIP-10140N
IntActiP77791, 16 interactors
STRINGi511145.b0459

2D gel databases

SWISS-2DPAGEiP77791

Proteomic databases

jPOSTiP77791
PaxDbiP77791
PRIDEiP77791

Genome annotation databases

EnsemblBacteriaiAAC73561; AAC73561; b0459
BAE76238; BAE76238; BAE76238
GeneIDi58460091
945096
KEGGiecj:JW0448
eco:b0459
PATRICifig|1411691.4.peg.1817

Organism-specific databases

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

More...EchoBASEi		EB3990

Phylogenomic databases

eggNOGiCOG0110, Bacteria
HOGENOMiCLU_051638_3_3_6
InParanoidiP77791
PhylomeDBiP77791

Enzyme and pathway databases

BioCyciEcoCyc:MALTACETYLTRAN-MONOMER
MetaCyc:MALTACETYLTRAN-MONOMER
BRENDAi2.3.1.79, 2026

Miscellaneous databases

EvolutionaryTraceiP77791

Protein Ontology

More...PROi		PR:P77791

Family and domain databases

InterProiView protein in InterPro
IPR001451, Hexapep
IPR018357, Hexapep_transf_CS
IPR024688, Mac_dom
IPR011004, Trimer_LpxA-like_sf
PfamiView protein in Pfam
PF14602, Hexapep_2, 2 hits
PF12464, Mac, 1 hit
SMARTiView protein in SMART
SM01266, Mac, 1 hit
SUPFAMiSSF51161, SSF51161, 1 hit
PROSITEiView protein in PROSITE
PS00101, HEXAPEP_TRANSFERASES, 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 nameiMAA_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: P77791
Secondary accession number(s): Q2MBW8
<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: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 151 of the entry and version 3 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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