GLDSA_STRKN
ID GLDSA_STRKN Reviewed; 427 AA.
AC Q6L739;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=L-glutamine:2-deoxy-scyllo-inosose aminotransferase;
DE Short=L-glutamine:DOI aminotransferase;
DE EC=2.6.1.100 {ECO:0000269|PubMed:19219581, ECO:0000269|PubMed:21983602};
DE AltName: Full=L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase;
DE Short=L-glutamine:amino-DOI aminotransferase;
DE EC=2.6.1.101 {ECO:0000269|PubMed:19219581, ECO:0000269|PubMed:21983602};
GN Name=kanB; Synonyms=kanS1;
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, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC Ac-837;
RX PubMed=19219581; DOI=10.1007/s10529-009-9937-0;
RA Jnawali H.N., Subba B., Liou K., Sohng J.K.;
RT "Functional characterization of kanB by complementing in engineered
RT Streptomyces fradiae Deltaneo6::tsr.";
RL Biotechnol. Lett. 31:869-875(2009).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21983602; DOI=10.1038/nchembio.671;
RA Park J.W., Park S.R., Nepal K.K., Han A.R., Ban Y.H., Yoo Y.J., Kim E.J.,
RA Kim E.M., Kim D., Sohng J.K., Yoon Y.J.;
RT "Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic
RT manipulation.";
RL Nat. Chem. Biol. 7:843-852(2011).
CC -!- FUNCTION: Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-
CC inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L-
CC glutamine as the amino donor. Also catalyzes the transamination of 3-
CC amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine
CC (2-DOS). {ECO:0000269|PubMed:19219581, ECO:0000269|PubMed:21983602}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-L-scyllo-inosose + L-glutamine = 2-deoxy-scyllo-
CC inosamine + 2-oxoglutaramate; Xref=Rhea:RHEA:34147,
CC ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:64796,
CC ChEBI:CHEBI:65003; EC=2.6.1.100;
CC Evidence={ECO:0000269|PubMed:19219581, ECO:0000269|PubMed:21983602};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-amino-2,3-dideoxy-scyllo-inosose + L-glutamine = 2-
CC deoxystreptamine + 2-oxoglutaramate; Xref=Rhea:RHEA:34151,
CC ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:65002,
CC ChEBI:CHEBI:65069; EC=2.6.1.101;
CC Evidence={ECO:0000269|PubMed:19219581, ECO:0000269|PubMed:21983602};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 2/4.
CC -!- PATHWAY: Antibiotic biosynthesis; kanamycin biosynthesis.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. L-glutamine:2-deoxy-
CC scyllo-inosose/scyllo-inosose aminotransferase subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ582817; CAE46938.1; -; Genomic_DNA.
DR EMBL; AB164642; BAD20758.1; -; Genomic_DNA.
DR EMBL; AJ628422; CAF31588.1; -; Genomic_DNA.
DR RefSeq; WP_055553821.1; NZ_LIQU01000374.1.
DR AlphaFoldDB; Q6L739; -.
DR SMR; Q6L739; -.
DR KEGG; ag:CAE46938; -.
DR OrthoDB; 1722208at2; -.
DR BioCyc; MetaCyc:MON-17185; -.
DR BRENDA; 2.6.1.100; 6046.
DR UniPathway; UPA00907; UER00922.
DR UniPathway; UPA00965; -.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..427
FT /note="L-glutamine:2-deoxy-scyllo-inosose aminotransferase"
FT /id="PRO_0000233019"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 45870 MW; F2F738CC5AD4C7B2 CRC64;
MPLQSSRLAV DNGTPVRGKP WPVWPQPTDG TLDALSRVLR SGRWAISGPY RGVESAERRF
ARRFADYHRI AHCVPASSGT ASLMLALEAC GVGAGDEVIL PGVTWVASAS TVVGVNAVPV
FADIDPDTLC LDPDAVEAAI TPATKAIVVV HLYAAVADLT RLKEVADRHG IVLIEDCAQA
HGAEFEGHKV GTFGAVGTFS MQQSKVLTSG EGGAAITADP VLARRMEHLR ADGRCYRDQA
PPSGHMELVE TGELMGSNRC ISEFQAAVLT EQLGELDRFN ALRRHNAELL DALLTDVGYR
PQRSTPGTTA RTYYTYVAEL PDAELPGADI TKVTEALTAE LGFPVAPAYS PLNANPLYDP
ASRSRFALGP QHEKLIDPAR FVLPVSGRLT RRLVTFHHAA LLGDESDMRD IAEAFTKVLQ
HRAVLAA
