MAA_ECOLI
ID MAA_ECOLI Reviewed; 183 AA.
AC P77791; Q2MBW8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Maltose O-acetyltransferase {ECO:0000303|PubMed:12731863};
DE Short=MAT {ECO:0000303|PubMed:12731863};
DE EC=2.3.1.79 {ECO:0000269|PubMed:12731863, ECO:0000269|PubMed:1856235};
DE AltName: Full=Maltose transacetylase {ECO:0000303|PubMed:1856235};
GN Name=maa; Synonyms=ylaD; OrderedLocusNames=b0459, JW0448;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RA Boehm A.S.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=1856235; DOI=10.1016/s0021-9258(18)92816-4;
RA Brand B., Boos W.;
RT "Maltose transacetylase of Escherichia coli. Mapping and cloning of its
RT structural, gene, mac, and characterization of the enzyme as a dimer of
RT identical polypeptides with a molecular weight of 20,000.";
RL J. Biol. Chem. 266:14113-14118(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12731863; DOI=10.1021/bi0271446;
RA Lo Leggio L., Dal Degan F., Poulsen P., Andersen S.M., Larsen S.;
RT "The structure and specificity of Escherichia coli maltose
RT acetyltransferase give new insight into the LacA family of
RT acyltransferases.";
RL Biochemistry 42:5225-5235(2003).
CC -!- FUNCTION: Catalyzes the CoA-dependent transfer of an acetyl group to
CC maltose and other sugars (PubMed:1856235). Acetylates glucose
CC exclusively at the C6 position and maltose at the C6 position of the
CC non-reducing end glucosyl moiety. Is able to acetylate
CC maltooligosaccharides (PubMed:12731863). {ECO:0000269|PubMed:12731863,
CC ECO:0000269|PubMed:1856235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + D-maltose = 1-O-acetylmaltose + CoA;
CC Xref=Rhea:RHEA:10456, ChEBI:CHEBI:13714, ChEBI:CHEBI:17306,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.79;
CC Evidence={ECO:0000269|PubMed:12731863, ECO:0000269|PubMed:1856235};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 mM for glucose {ECO:0000269|PubMed:1856235};
CC KM=90 mM for maltose {ECO:0000269|PubMed:1856235};
CC KM=71 mM for glucose {ECO:0000269|PubMed:12731863};
CC KM=42.9 mM for maltose {ECO:0000269|PubMed:12731863};
CC KM=285.5 mM for maltotriose {ECO:0000269|PubMed:12731863};
CC Vmax=0.20 mmol/min/mg enzyme with glucose as substrate
CC {ECO:0000269|PubMed:1856235};
CC Vmax=0.11 mmol/min/mg enzyme with maltose as substrate
CC {ECO:0000269|PubMed:1856235};
CC Note=Acetylates glucose, maltose, mannose, galactose, and fructose
CC with a decreasing relative rate of 1, 0.55, 0.20, 0.07, 0.04.
CC {ECO:0000269|PubMed:1856235};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:12731863};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1856235}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; AJ223173; CAA11147.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40214.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73561.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76238.1; -; Genomic_DNA.
DR PIR; B64776; B64776.
DR RefSeq; NP_414992.1; NC_000913.3.
DR RefSeq; WP_000102564.1; NZ_SSUW01000008.1.
DR PDB; 1OCX; X-ray; 2.15 A; A/B/C=2-183.
DR PDB; 6AG8; X-ray; 1.34 A; A/C=1-183.
DR PDBsum; 1OCX; -.
DR PDBsum; 6AG8; -.
DR AlphaFoldDB; P77791; -.
DR SMR; P77791; -.
DR BioGRID; 4261202; 4.
DR DIP; DIP-10140N; -.
DR IntAct; P77791; 16.
DR STRING; 511145.b0459; -.
DR SWISS-2DPAGE; P77791; -.
DR jPOST; P77791; -.
DR PaxDb; P77791; -.
DR PRIDE; P77791; -.
DR EnsemblBacteria; AAC73561; AAC73561; b0459.
DR EnsemblBacteria; BAE76238; BAE76238; BAE76238.
DR GeneID; 58460091; -.
DR GeneID; 945096; -.
DR KEGG; ecj:JW0448; -.
DR KEGG; eco:b0459; -.
DR PATRIC; fig|1411691.4.peg.1817; -.
DR EchoBASE; EB3990; -.
DR eggNOG; COG0110; Bacteria.
DR HOGENOM; CLU_051638_3_3_6; -.
DR InParanoid; P77791; -.
DR OMA; DCQIGPN; -.
DR PhylomeDB; P77791; -.
DR BioCyc; EcoCyc:MALTACETYLTRAN-MON; -.
DR BioCyc; MetaCyc:MALTACETYLTRAN-MON; -.
DR BRENDA; 2.3.1.79; 2026.
DR EvolutionaryTrace; P77791; -.
DR PRO; PR:P77791; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008925; F:maltose O-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR024688; Mac_dom.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF14602; Hexapep_2; 2.
DR Pfam; PF12464; Mac; 1.
DR SMART; SM01266; Mac; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9600841"
FT CHAIN 2..183
FT /note="Maltose O-acetyltransferase"
FT /id="PRO_0000068729"
FT ACT_SITE 113
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 83
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 140
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 158
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 163..164
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 178
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 181
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT SITE 83
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:6AG8"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:6AG8"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6AG8"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:6AG8"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:6AG8"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6AG8"
SQ SEQUENCE 183 AA; 20096 MW; 3E4C7A4D68AA49C4 CRC64;
MSTEKEKMIA GELYRSADET LSRDRLRARQ LIHRYNHSLA EEHTLRQQIL ADLFGQVTEA
YIEPTFRCDY GYNIFLGNNF FANFDCVMLD VCPIRIGDNC MLAPGVHIYT ATHPIDPVAR
NSGAELGKPV TIGNNVWIGG RAVINPGVTI GDNVVVASGA VVTKDVPDNV VVGGNPARII
KKL
