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Protein

Maltose O-acetyltransferase

Gene

maa

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates maltose and other sugars.

Catalytic activityi

Acetyl-CoA + maltose = CoA + acetyl-maltose.

Kineticsi

Acetylates glucose, maltose, mannose, galactose, and fructose with a decreasing relative rate of 1, 0.55, 0.20, 0.07, 0.04.

  1. KM=62 mM for glucose
  2. KM=90 mM for maltose
  1. Vmax=0.20 mmol/min/mg enzyme with glucose as substrate
  2. Vmax=0.11 mmol/min/mg enzyme with maltose as substrate

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • maltose O-acetyltransferase activity Source: EcoCyc

GO - Biological processi

  • protein homotrimerization Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:MALTACETYLTRAN-MONOMER.
ECOL316407:JW0448-MONOMER.
MetaCyc:MALTACETYLTRAN-MONOMER.
BRENDAi2.3.1.79. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Maltose O-acetyltransferase (EC:2.3.1.79)
Alternative name(s):
Maltose transacetylase
Gene namesi
Name:maa
Synonyms:ylaD
Ordered Locus Names:b0459, JW0448
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14239. maa.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 183182Maltose O-acetyltransferasePRO_0000068729Add
BLAST

Proteomic databases

PaxDbiP77791.

2D gel databases

SWISS-2DPAGEP77791.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261202. 4 interactions.
DIPiDIP-10140N.
IntActiP77791. 16 interactions.
STRINGi511145.b0459.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Helixi19 – 3719Combined sources
Helixi43 – 5311Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 625Combined sources
Beta strandi66 – 716Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 825Combined sources
Beta strandi84 – 896Combined sources
Beta strandi94 – 963Combined sources
Beta strandi107 – 1093Combined sources
Helixi117 – 1204Combined sources
Turni121 – 1233Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi168 – 1736Combined sources
Turni174 – 1774Combined sources
Beta strandi178 – 1825Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCXX-ray2.15A/B/C2-183[»]
ProteinModelPortaliP77791.
SMRiP77791. Positions 2-183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77791.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108UW5. Bacteria.
COG0110. LUCA.
HOGENOMiHOG000049435.
InParanoidiP77791.
KOiK00661.
OMAiVFLNFNC.
OrthoDBiEOG6HB9VW.
PhylomeDBiP77791.

Family and domain databases

InterProiIPR001451. Hexapep.
IPR018357. Hexapep_transf_CS.
IPR024688. Mac_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF14602. Hexapep_2. 2 hits.
PF12464. Mac. 1 hit.
[Graphical view]
SMARTiSM01266. Mac. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i3E4C7A4D68AA49C4
GO

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_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73561; AAC73561; b0459.
BAE76238; BAE76238; BAE76238.
GeneIDi945096.
KEGGiecj:JW0448.
eco:b0459.
PATRICi32116071. VBIEscCol129921_0477.

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_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OCXX-ray2.15A/B/C2-183[»]
ProteinModelPortaliP77791.
SMRiP77791. Positions 2-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261202. 4 interactions.
DIPiDIP-10140N.
IntActiP77791. 16 interactions.
STRINGi511145.b0459.

2D gel databases

SWISS-2DPAGEP77791.

Proteomic databases

PaxDbiP77791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73561; AAC73561; b0459.
BAE76238; BAE76238; BAE76238.
GeneIDi945096.
KEGGiecj:JW0448.
eco:b0459.
PATRICi32116071. VBIEscCol129921_0477.

Organism-specific databases

EchoBASEiEB3990.
EcoGeneiEG14239. maa.

Phylogenomic databases

eggNOGiENOG4108UW5. Bacteria.
COG0110. LUCA.
HOGENOMiHOG000049435.
InParanoidiP77791.
KOiK00661.
OMAiVFLNFNC.
OrthoDBiEOG6HB9VW.
PhylomeDBiP77791.

Enzyme and pathway databases

BioCyciEcoCyc:MALTACETYLTRAN-MONOMER.
ECOL316407:JW0448-MONOMER.
MetaCyc:MALTACETYLTRAN-MONOMER.
BRENDAi2.3.1.79. 2026.

Miscellaneous databases

EvolutionaryTraceiP77791.
PROiP77791.

Family and domain databases

InterProiIPR001451. Hexapep.
IPR018357. Hexapep_transf_CS.
IPR024688. Mac_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF14602. Hexapep_2. 2 hits.
PF12464. Mac. 1 hit.
[Graphical view]
SMARTiSM01266. Mac. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Boehm A.S.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural, gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20,000."
    Brand B., Boos W.
    J. Biol. Chem. 266:14113-14118(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiMAA_ECOLI
AccessioniPrimary (citable) accession number: P77791
Secondary accession number(s): Q2MBW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.