Y3168_MYCTU
ID Y3168_MYCTU Reviewed; 378 AA.
AC P9WI99; F2GJM6; L0TES4; O53318; Q7D606;
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=Putative aminoglycoside phosphotransferase;
DE EC=2.7.1.-;
DE AltName: Full=Putative aminoglycoside antibiotics resistance enzyme;
GN OrderedLocusNames=Rv3168;
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 [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 [2]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21543877; DOI=10.1107/s1744309111010487;
RA Kim S., Nguyen C.M., Yeo S.J., Ahn J.W., Kim E.J., Kim K.J.;
RT "Cloning, expression, purification, crystallization and X-ray
RT crystallographic analysis of Rv3168 from Mycobacterium tuberculosis
RT H37Rv.";
RL Acta Crystallogr. F 67:627-629(2011).
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 (1.67 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH ATP
RP AND MAGNESIUM, PUTATIVE FUNCTION, AND ACTIVE SITE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21905120; DOI=10.1002/prot.23119;
RA Kim S., Nguyen C.M., Kim E.J., Kim K.J.;
RT "Crystal structure of Mycobacterium tuberculosis Rv3168: a putative
RT aminoglycoside antibiotics resistance enzyme.";
RL Proteins 79:2983-2987(2011).
CC -!- FUNCTION: Might catalyze the phosphorylation of aminoglycosides and
CC confer aminoglycoside antibiotics resistance.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45979.1; -; Genomic_DNA.
DR PIR; F70947; F70947.
DR RefSeq; NP_217684.1; NC_000962.3.
DR RefSeq; WP_003900650.1; NZ_NVQJ01000019.1.
DR PDB; 3ATS; X-ray; 1.67 A; A=22-378.
DR PDB; 3ATT; X-ray; 2.00 A; A=22-378.
DR PDBsum; 3ATS; -.
DR PDBsum; 3ATT; -.
DR AlphaFoldDB; P9WI99; -.
DR SMR; P9WI99; -.
DR STRING; 83332.Rv3168; -.
DR PaxDb; P9WI99; -.
DR DNASU; 888778; -.
DR GeneID; 45427156; -.
DR GeneID; 888778; -.
DR KEGG; mtu:Rv3168; -.
DR TubercuList; Rv3168; -.
DR eggNOG; COG3173; Bacteria.
DR OMA; WYDFAVP; -.
DR PhylomeDB; P9WI99; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..378
FT /note="Putative aminoglycoside phosphotransferase"
FT /id="PRO_0000420881"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21905120"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:21905120"
FT BINDING 134..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:21905120"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21905120"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21905120"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21905120"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21905120"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 53..67
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3ATS"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3ATS"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3ATS"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 198..217
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3ATS"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 277..296
FT /evidence="ECO:0007829|PDB:3ATS"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:3ATT"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 327..350
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:3ATS"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:3ATS"
SQ SEQUENCE 378 AA; 42561 MW; D1606BF6514E179A CRC64;
MANEPAIGAI DRLQRSSRDV TTLPAVISRW LSSVLPGGAA PEVTVESGVD STGMSSETII
LTARWQQDGR SIQQKLVARV APAAEDVPVF PTYRLDHQFE VIRLVGELTD VPVPRVRWIE
TTGDVLGTPF FLMDYVEGVV PPDVMPYTFG DNWFADAPAE RQRQLQDATV AALATLHSIP
NAQNTFSFLT QGRTSDTTLH RHFNWVRSWY DFAVEGIGRS PLLERTFEWL QSHWPDDAAA
REPVLLWGDA RVGNVLYRDF QPVAVLDWEM VALGPRELDV AWMIFAHRVF QELAGLATLP
GLPEVMREDD VRATYQALTG VELGDLHWFY VYSGVMWACV FMRTGARRVH FGEIEKPDDV
ESLFYHAGLM KHLLGEEH
