MAA_BACSU
ID MAA_BACSU Reviewed; 184 AA.
AC P37515;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable maltose O-acetyltransferase;
DE EC=2.3.1.79;
DE AltName: Full=Maltose transacetylase;
GN Name=maa; Synonyms=yyaI; OrderedLocusNames=BSU40850;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BD99;
RX PubMed=8011666; DOI=10.1016/0005-2728(94)90131-7;
RA Quirk P.G., Guffanti A.A., Clejan S., Cheng J., Krulwich T.A.;
RT "Isolation of Tn917 insertional mutants of Bacillus subtilis that are
RT resistant to the protonophore carbonyl cyanide m-chlorophenylhydrazone.";
RL Biochim. Biophys. Acta 1186:27-34(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Catalyzes the CoA-dependent transfer of an acetyl group to
CC maltose and other sugars. Acetylates glucose exclusively at the C6
CC position and maltose at the C6 position of the non-reducing end
CC glucosyl moiety. Is able to acetylate maltooligosaccharides.
CC {ECO:0000250|UniProtKB:P77791}.
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:0000250|UniProtKB:P77791};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P77791}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; D26185; BAA05215.1; -; Genomic_DNA.
DR EMBL; L16865; AAA64343.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16122.1; -; Genomic_DNA.
DR PIR; I39920; I39920.
DR RefSeq; NP_391965.1; NC_000964.3.
DR RefSeq; WP_003242928.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P37515; -.
DR SMR; P37515; -.
DR STRING; 224308.BSU40850; -.
DR PaxDb; P37515; -.
DR PRIDE; P37515; -.
DR EnsemblBacteria; CAB16122; CAB16122; BSU_40850.
DR GeneID; 937913; -.
DR KEGG; bsu:BSU40850; -.
DR PATRIC; fig|224308.179.peg.4426; -.
DR eggNOG; COG0110; Bacteria.
DR InParanoid; P37515; -.
DR OMA; YHIHIGD; -.
DR PhylomeDB; P37515; -.
DR BioCyc; BSUB:BSU40850-MON; -.
DR BRENDA; 2.3.1.79; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008925; F:maltose O-acetyltransferase activity; IEA:UniProtKB-EC.
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; 1.
DR Pfam; PF12464; Mac; 1.
DR SMART; SM01266; Mac; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..184
FT /note="Probable maltose O-acetyltransferase"
FT /id="PRO_0000068730"
FT ACT_SITE 114
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07464"
FT BINDING 84
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 141
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 159
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 164..165
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 179
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 182
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 84
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P07464"
SQ SEQUENCE 184 AA; 20210 MW; A85F307E5488BD1D CRC64;
MLRTEKEKMA AGELYNSEDQ QLLLERKHAR QLIRQYNETP EDDAVRTKLL KELLGSVGDQ
VTILPTFRCD YGYHIHIGDH TFVNFDCVIL DVCEVRIGCH CLIAPGVHIY TAGHPLDPIE
RKSGKEFGKP VTIGDQVWIG GRAVINPGVT IGDNAVIASG SVVTKDVPAN TVVGGNPARI
LKQL
