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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
 
 
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