ID   A0A3P1UCA6_BACAN        Unreviewed;       265 AA.
AC   A0A3P1UCA6; E9R7S1; Q6KRH6; Q81P86;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Aminoglycoside N(3)-acetyltransferase {ECO:0000256|RuleBase:RU365031};
DE            EC=2.3.1.81 {ECO:0000256|RuleBase:RU365031};
GN   Name=aacC7 {ECO:0000313|EMBL:AAT32047.1};
GN   OrderedLocusNames=GBAA_2930 {ECO:0000313|EMBL:AAT32047.1};
OS   Bacillus anthracis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT32047.1, ECO:0000313|Proteomes:UP000000594};
RN   [1] {ECO:0000313|EMBL:AAT32047.1, ECO:0000313|Proteomes:UP000000594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594};
RX   PubMed=18952800; DOI=10.1128/JB.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [2] {ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACETYL-COA.
RX   PubMed=21601576; DOI=10.1016/j.jmb.2011.04.076;
RA   Klimecka M.M., Chruszcz M., Font J., Skarina T., Shumilin I.,
RA   Onopryienko O., Porebski P.J., Cymborowski M., Zimmerman M.D., Hasseman J.,
RA   Glomski I.J., Lebioda L., Savchenko A., Edwards A., Minor W.;
RT   "Structural analysis of a putative aminoglycoside N-acetyltransferase from
RT   Bacillus anthracis.";
RL   J. Mol. Biol. 410:411-423(2011).
RN   [3] {ECO:0007829|PDB:3SLB}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACETYL-COA AND
RP   CYTOSINE.
RA   Klimecka M.M., Chruszcz M., Porebski P.J., Cymborowski M., Anderson W.,
RA   Minor W.;
RT   "Crystal structure of BA2930 in complex with AcCoA and cytosine.";
RL   Submitted (JUN-2011) to the PDB data bank.
RN   [4] {ECO:0007829|PDB:3SLF}
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH ACETYL-COA.
RG   Center for Structural Genomics of Infectious Diseases (CSGID);
RA   Klimecka M.M., Chruszcz M., Porebski P.J., Cymborowski M., Anderson W.,
RA   Minor W.;
RT   "Crystal structure of BA2930 in complex with AcCoA and uracil.";
RL   Submitted (JUN-2011) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-deoxystreptamine antibiotic + acetyl-CoA = an N(3')-
CC         acetyl-2-deoxystreptamine antibiotic + CoA + H(+);
CC         Xref=Rhea:RHEA:12665, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57921, ChEBI:CHEBI:77452; EC=2.3.1.81;
CC         Evidence={ECO:0000256|RuleBase:RU365031};
CC   -!- SIMILARITY: Belongs to the antibiotic N-acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006383, ECO:0000256|RuleBase:RU365031}.
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DR   EMBL; AE017334; AAT32047.1; -; Genomic_DNA.
DR   RefSeq; WP_009879231.1; NZ_WXXJ01000026.1.
DR   PDB; 3IJW; X-ray; 1.90 A; A/B=1-265.
DR   PDB; 3N0M; X-ray; 2.40 A; A/B=1-265.
DR   PDB; 3N0S; X-ray; 2.15 A; A/B/C/D=1-265.
DR   PDB; 3SLB; X-ray; 2.00 A; A/B/C/D=1-265.
DR   PDB; 3SLF; X-ray; 2.05 A; A/B=1-265.
DR   AlphaFoldDB; A0A3P1UCA6; -.
DR   SMR; A0A3P1UCA6; -.
DR   GeneID; 45022749; -.
DR   KEGG; bar:GBAA_2930; -.
DR   OrthoDB; 7330654at2; -.
DR   Proteomes; UP000000594; Chromosome.
DR   GO; GO:0046353; F:aminoglycoside 3-N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR003679; Amioglycoside_AcTrfase.
DR   InterPro; IPR028345; Antibiotic_NAT-like.
DR   PANTHER; PTHR11104; AMINOGLYCOSIDE N3-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR11104:SF0; SPBETA PROPHAGE-DERIVED AMINOGLYCOSIDE N(3')-ACETYLTRANSFERASE-LIKE PROTEIN YOKD; 1.
DR   Pfam; PF02522; Antibiotic_NAT; 1.
DR   SUPFAM; SSF110710; TTHA0583/YokD-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU365031};
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW   ECO:0000256|RuleBase:RU365031};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000594};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365031}.
FT   BINDING         35
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         36
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         37
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         38
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         39
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         44
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         70
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         80
FT                   /ligand="cytosine"
FT                   /ligand_id="ChEBI:CHEBI:16040"
FT                   /evidence="ECO:0007829|PDB:3SLB"
FT   BINDING         81
FT                   /ligand="cytosine"
FT                   /ligand_id="ChEBI:CHEBI:16040"
FT                   /evidence="ECO:0007829|PDB:3SLB"
FT   BINDING         82
FT                   /ligand="cytosine"
FT                   /ligand_id="ChEBI:CHEBI:16040"
FT                   /evidence="ECO:0007829|PDB:3SLB"
FT   BINDING         83
FT                   /ligand="cytosine"
FT                   /ligand_id="ChEBI:CHEBI:16040"
FT                   /evidence="ECO:0007829|PDB:3SLB"
FT   BINDING         109
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3N0M"
FT   BINDING         112
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         178
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
FT   BINDING         180
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0007829|PDB:3IJW, ECO:0007829|PDB:3N0M"
SQ   SEQUENCE   265 AA;  29608 MW;  4D116A8480798FF7 CRC64;
     MNDIVASTQL PNTIKTITND LRKLGLKKGM TVIVHSSLSS IGWISGGAVA VVEALMEVIT
     EEGTIIMPTQ SSDLSDPKHW SRPPVPEEWW QIIRDNVPAF EPHITPTRAM GKVVECFRTY
     PNVVRSNHPL GSFAAWGRHA EEITVNQSLS MSLGEESPLR KIYDLDGYIL LIGVGYDSNT
     SVHLSEVRSG ACELIKVGAP IIENGERVWK EFVDMDYDSD KFVEIGVEFE QKGTVTMGKI
     GNAKCRLMKQ RDIVDFGTEW FRKKN
//