ID G8PU14_PSEUV Unreviewed; 260 AA.
AC G8PU14;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Aminoglycoside 3'-phosphotransferase {ECO:0000256|ARBA:ARBA00017903};
DE EC=2.7.1.95 {ECO:0000256|ARBA:ARBA00012193};
GN Name=neo {ECO:0000313|EMBL:AEV38766.1};
GN OrderedLocusNames=PSE_4262 {ECO:0000313|EMBL:AEV38766.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38766.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV38766.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38766.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + kanamycin A = ADP + H(+) + kanamycin 3'-phosphate;
CC Xref=Rhea:RHEA:24256, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57909, ChEBI:CHEBI:58214, ChEBI:CHEBI:456216;
CC EC=2.7.1.95; Evidence={ECO:0000256|ARBA:ARBA00001685};
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219, ECO:0000256|PIRNR:PIRNR000706}.
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DR EMBL; CP003147; AEV38766.1; -; Genomic_DNA.
DR RefSeq; WP_014286608.1; NC_016642.1.
DR AlphaFoldDB; G8PU14; -.
DR STRING; 911045.PSE_4262; -.
DR KEGG; psf:PSE_4262; -.
DR eggNOG; COG3231; Bacteria.
DR HOGENOM; CLU_073027_0_1_5; -.
DR Proteomes; UP000005634; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008910; F:kanamycin kinase activity; IEA:UniProtKB-EC.
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; cd05150; APH; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR024165; Kan/Strep_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR PIRSF; PIRSF000706; Kanamycin_kin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|PIRNR:PIRNR000706};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000706};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000706};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000706-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000706-2};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000706};
KW Transferase {ECO:0000256|PIRNR:PIRNR000706, ECO:0000313|EMBL:AEV38766.1}.
FT DOMAIN 24..248
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-1"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000706-2"
SQ SEQUENCE 260 AA; 29870 MW; A86160A023D33C47 CRC64;
MHNLNFPPEI QCRLRSYDWH KDSMGRSASD IFMLTQNGDL KLVLKVEQDG PFAELSDEAK
RLEWLTERGV LCPEVQWFEQ YEGRQWLLLT ALSGTDLVSD PELLPLQQVE ILADALRHLH
TLDWEGCPYD QTVELGLREA EARMKAGLVN EDDFDPEWQG EPAQKLFSYL TANIPEVHEK
VLCHGDACLP NFMATAGDFS GYLDCSRVGL ADRYQDLALA VRSIRYNHDD AAVEHFLKCY
GIEQFDKKRA TFFTTLDEFF
//
