AAC2_MYCTU
ID AAC2_MYCTU Reviewed; 181 AA.
AC P9WQG9; L0T655; P0A5N0; P72033; P95219;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Aminoglycoside 2'-N-acetyltransferase;
DE EC=2.3.1.-;
DE AltName: Full=AAC(2')-Ic {ECO:0000303|PubMed:9159528};
GN Name=aac; OrderedLocusNames=Rv0262c; ORFNames=MTCY06A4.06c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9159528; DOI=10.1046/j.1365-2958.1997.3471717.x;
RA Ainsa J.A., Perez E., Pelicic V., Berthet F.-X., Gicquel B., Martin C.;
RT "Aminoglycoside 2'-N-acetyltransferase genes are universally present in
RT mycobacteria: characterization of the aac(2')-Ic gene from Mycobacterium
RT tuberculosis and the aac(2')-Id gene from Mycobacterium smegmatis.";
RL Mol. Microbiol. 24:431-441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH COENZYME A;
RP RIBOSTAMYCIN; KANAMYCIN AND TOBRAMYCIN, AND SUBUNIT.
RX PubMed=12161746; DOI=10.1038/nsb830;
RA Vetting M.W., Hegde S.S., Javid-Majd F., Blanchard J.S., Roderick S.L.;
RT "Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in
RT complex with coenzyme A and aminoglycoside substrates.";
RL Nat. Struct. Biol. 9:653-658(2002).
CC -!- FUNCTION: May catalyze the coenzyme A-dependent acetylation of the 2'
CC hydroxyl or amino group of a broad spectrum of aminoglycosides and
CC confer resistance to aminoglycosides (By similarity). In vitro assays
CC show no significant increase of resistance to aminoglycosides, possibly
CC due to low expression in a heterologous system (PubMed:9159528).
CC {ECO:0000250|UniProtKB:P94968, ECO:0000269|PubMed:9159528}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12161746}.
CC -!- SIMILARITY: Belongs to the AAC(2')-I acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U72714; AAB17563.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP42991.1; -; Genomic_DNA.
DR PIR; A70627; A70627.
DR RefSeq; NP_214776.1; NC_000962.3.
DR RefSeq; WP_003899880.1; NZ_NVQJ01000055.1.
DR PDB; 1M44; X-ray; 1.60 A; A/B=1-181.
DR PDB; 1M4D; X-ray; 1.80 A; A/B=1-181.
DR PDB; 1M4G; X-ray; 1.80 A; A/B=1-181.
DR PDB; 1M4I; X-ray; 1.50 A; A/B=1-181.
DR PDBsum; 1M44; -.
DR PDBsum; 1M4D; -.
DR PDBsum; 1M4G; -.
DR PDBsum; 1M4I; -.
DR AlphaFoldDB; P9WQG9; -.
DR SMR; P9WQG9; -.
DR STRING; 83332.Rv0262c; -.
DR ChEMBL; CHEMBL3708053; -.
DR DrugBank; DB01842; 3'-Phosphate-Adenosine-5'-Diphosphate.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB01172; Kanamycin.
DR DrugBank; DB03615; Ribostamycin.
DR PaxDb; P9WQG9; -.
DR DNASU; 886648; -.
DR GeneID; 45424234; -.
DR GeneID; 886648; -.
DR KEGG; ag:AAB17563; -.
DR KEGG; mtu:Rv0262c; -.
DR TubercuList; Rv0262c; -.
DR eggNOG; COG0456; Bacteria.
DR OMA; VFDWRDG; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0047921; F:aminoglycoside 2'-N-acetyltransferase activity; IDA:MTBBASE.
DR GO; GO:0034069; F:aminoglycoside N-acetyltransferase activity; IDA:MTBBASE.
DR GO; GO:0030649; P:aminoglycoside antibiotic catabolic process; IDA:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic resistance; Reference proteome;
KW Transferase.
FT CHAIN 1..181
FT /note="Aminoglycoside 2'-N-acetyltransferase"
FT /id="PRO_0000064412"
FT DOMAIN 11..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12161746"
FT BINDING 82..83
FT /ligand="substrate"
FT BINDING 84..86
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:12161746,
FT ECO:0007744|PDB:1M4D, ECO:0007744|PDB:1M4G,
FT ECO:0007744|PDB:1M4I"
FT BINDING 91..96
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:12161746,
FT ECO:0007744|PDB:1M4D, ECO:0007744|PDB:1M4G,
FT ECO:0007744|PDB:1M4I"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12161746"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12161746"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1M4I"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1M4I"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:1M4I"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1M4I"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 57..71
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 74..86
FT /evidence="ECO:0007829|PDB:1M4I"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1M4I"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1M4I"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1M4I"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1M4I"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1M4I"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1M4I"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1M4I"
SQ SEQUENCE 181 AA; 20038 MW; A5F553E9DCBF1F0A CRC64;
MHTQVHTARL VHTADLDSET RQDIRQMVTG AFAGDFTETD WEHTLGGMHA LIWHHGAIIA
HAAVIQRRLI YRGNALRCGY VEGVAVRADW RGQRLVSALL DAVEQVMRGA YQLGALSSSA
RARRLYASRG WLPWHGPTSV LAPTGPVRTP DDDGTVFVLP IDISLDTSAE LMCDWRAGDV
W
