KANK_STRKN
ID KANK_STRKN Reviewed; 352 AA.
AC Q2MFU6; Q65CC3; Q6L731;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=2'-dehydrokanamycin reductase;
DE EC=1.1.1.355;
DE AltName: Full=Kanamycin biosynthesis protein K;
GN Name=kanK; Synonyms=kacC;
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, 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 2'-dehydrokanamycin A into
CC kanamycin A. {ECO:0000269|PubMed:22374809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-dehydrokanamycin A + H(+) + NADPH = kanamycin A + NADP(+);
CC Xref=Rhea:RHEA:35835, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58214, ChEBI:CHEBI:58349, ChEBI:CHEBI:72757;
CC EC=1.1.1.355; Evidence={ECO:0000269|PubMed:22374809};
CC -!- PATHWAY: Antibiotic biosynthesis; kanamycin biosynthesis.
CC {ECO:0000269|PubMed:22374809}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE46945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAF31595.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ582817; CAE46945.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB164642; BAD20766.1; -; Genomic_DNA.
DR EMBL; AJ628422; CAF31595.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q2MFU6; -.
DR SMR; Q2MFU6; -.
DR KEGG; ag:BAD20766; -.
DR BioCyc; MetaCyc:MON-17981; -.
DR BRENDA; 1.1.1.355; 6046.
DR UniPathway; UPA00965; -.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:1901133; P:kanamycin biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; NADP; Oxidoreductase.
FT CHAIN 1..352
FT /note="2'-dehydrokanamycin reductase"
FT /id="PRO_0000424127"
SQ SEQUENCE 352 AA; 37159 MW; 1A13FBBFC3E60848 CRC64;
MSSQLALRGP ELSANLCKPE EDTLRVLVTG GSGNVGVGVV RALNAARHHV VVASRGYSPA
LLPEGVRAVR LERTEPDAYT RLVAAEKPDA VIDLTCHDAA DAAVTLRACA GVDRVVVVSS
VTAAGPATTT PVTEATAAPP LSEYGIDKLA VEETVRAAWA DGTSQALLVR LGAVYRLGAD
LDGQLAEDGC WLAHAAAGAP AVLADDGAAR WNLLHADDAG AALAELLAND RARGVLVHLA
SRHPLPWREL YERVHHALGR PFNPVSVPAE WAAEQLEDAE FLAETSRWDQ VFDLGLLDRL
APSYQERGGP SRVTEVALWL IRQGRVGDAE LGAEIQELPA RLAAVRTAPG LV