KANJ_STRKN
ID KANJ_STRKN Reviewed; 285 AA.
AC Q6L732;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Kanamycin B dioxygenase;
DE EC=1.14.11.37;
DE AltName: Full=Kanamycin biosynthesis protein J;
GN Name=kanJ; Synonyms=kacB;
OS Streptomyces kanamyceticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1967;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC Ac-837;
RX PubMed=15313224; DOI=10.1016/j.abb.2004.06.009;
RA Kharel M.K., Subba B., Basnet D.B., Woo J.S., Lee H.C., Liou K.,
RA Sohng J.K.;
RT "A gene cluster for biosynthesis of kanamycin from Streptomyces
RT kanamyceticus: comparison with gentamicin biosynthetic gene cluster.";
RL Arch. Biochem. Biophys. 429:204-214(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=21-18;
RX PubMed=15303497; DOI=10.7164/antibiotics.57.351;
RA Yanai K., Murakami T.;
RT "The kanamycin biosynthetic gene cluster from Streptomyces kanamyceticus.";
RL J. Antibiot. 57:351-354(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC Ac-837;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Cloning and sequencing of the kanamycin biosynthetic gene cluster from
RT Streptomyces kanamyceticus DSM 40500.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC Ac-837;
RX PubMed=22374809; DOI=10.1002/anie.201108122;
RA Sucipto H., Kudo F., Eguchi T.;
RT "The last step of kanamycin biosynthesis: unique deamination reaction
RT catalyzed by the alpha-ketoglutarate-dependent nonheme iron dioxygenase
RT KanJ and the NADPH-dependent reductase KanK.";
RL Angew. Chem. Int. Ed. 51:3428-3431(2012).
CC -!- FUNCTION: Mediates the conversion of kanamycin B into 2'-
CC dehydrokanamycin A during the transformation of kanamycin B to
CC kanamycin A. {ECO:0000269|PubMed:22374809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + kanamycin B + O2 = 2'-dehydrokanamycin A +
CC CO2 + NH4(+) + succinate; Xref=Rhea:RHEA:35831, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58549, ChEBI:CHEBI:72757;
CC EC=1.14.11.37; Evidence={ECO:0000269|PubMed:22374809};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:22374809};
CC -!- PATHWAY: Antibiotic biosynthesis; kanamycin biosynthesis.
CC {ECO:0000269|PubMed:22374809}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; AB164642; BAD20765.1; -; Genomic_DNA.
DR EMBL; AJ582817; CAE46944.1; -; Genomic_DNA.
DR EMBL; AJ628422; CAF31594.2; -; Genomic_DNA.
DR RefSeq; WP_055555228.1; NZ_CP023699.1.
DR PDB; 6S0R; X-ray; 2.50 A; A/B/C/D/E/F=1-285.
DR PDB; 6S0S; X-ray; 2.40 A; A/B/C/D/E/F=1-285.
DR PDB; 6S0T; X-ray; 2.10 A; A/B/C/D/E/F=1-285.
DR PDB; 6S0U; X-ray; 2.15 A; A/B/C/D/E/F=1-277.
DR PDB; 6S0V; X-ray; 3.00 A; A/B/C/D/E/F=1-285.
DR PDB; 6S0W; X-ray; 2.36 A; A/B/C/D/E/F=1-285.
DR PDB; 7CL2; X-ray; 2.00 A; A/B/C/D/E/F=1-285.
DR PDB; 7CL3; X-ray; 2.20 A; A/B/C/D/E/F=1-285.
DR PDB; 7CL4; X-ray; 2.25 A; A/B/C/D/E/F=1-285.
DR PDB; 7CL5; X-ray; 2.50 A; A/B/C/D/E/F=1-285.
DR PDB; 7CL6; X-ray; 2.44 A; A/B/C/D/E/F=1-285.
DR PDBsum; 6S0R; -.
DR PDBsum; 6S0S; -.
DR PDBsum; 6S0T; -.
DR PDBsum; 6S0U; -.
DR PDBsum; 6S0V; -.
DR PDBsum; 6S0W; -.
DR PDBsum; 7CL2; -.
DR PDBsum; 7CL3; -.
DR PDBsum; 7CL4; -.
DR PDBsum; 7CL5; -.
DR PDBsum; 7CL6; -.
DR AlphaFoldDB; Q6L732; -.
DR SMR; Q6L732; -.
DR KEGG; ag:BAD20765; -.
DR OrthoDB; 1070946at2; -.
DR BioCyc; MetaCyc:MON-17980; -.
DR BRENDA; 1.14.11.37; 6046.
DR UniPathway; UPA00965; -.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:1901133; P:kanamycin biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Iron; Oxidoreductase.
FT CHAIN 1..285
FT /note="Kanamycin B dioxygenase"
FT /id="PRO_0000424136"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 47..65
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:7CL2"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6S0T"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:7CL2"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:7CL2"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:7CL2"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6S0S"
SQ SEQUENCE 285 AA; 31534 MW; CE3BE5E3F79FE8B9 CRC64;
MALAAPPGEL TLALTPDDKT LDPASLDRAL AILAEHGILV LTGMLRTRLT DQLRTAMLDD
LPEVLRQQDV PTNFVPGHVQ QDPPVRESLL FPDVLLNPVV YQITHAVLGA DARNAVYSGN
MNLPGSHEQP VHLDEPHLWP GISHPPYCLC VDVPLIDFTL ENGSTEYWPG SHVLNPDECY
DERGCVLPAE LERRRAVAPP VRFPIPVGSV VIRDGRLWHR GVPNLSAAPR PLLAMTHYTE
WFDMPPIQLP DTVKSWVDGS DRHTHAHFVA GDVDHLTGDH PFAVR
