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L-glutamine:2-deoxy-scyllo-inosose aminotransferase (L-glutamine:DOI aminotransferase) (EC 2.6.1.100) (Bifunctional L-glutamine:ketocyclitol aminotransferase I/II) (L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase) (L-glutamine:amino-DOI aminotransferase) (EC 2.6.1.101)

 GLDSA_STRFR             Reviewed;         424 AA.
Q53U20; Q6F6I2;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
28-FEB-2018, entry version 51.
RecName: Full=L-glutamine:2-deoxy-scyllo-inosose aminotransferase;
Short=L-glutamine:DOI aminotransferase;
EC=2.6.1.100 {ECO:0000250|UniProtKB:Q6L739};
AltName: Full=Bifunctional L-glutamine:ketocyclitol aminotransferase I/II;
AltName: Full=L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase;
Short=L-glutamine:amino-DOI aminotransferase;
EC=2.6.1.101 {ECO:0000250|UniProtKB:Q6L739};
Name=neoB; Synonyms=nemB, neo6, neoS, nmcS;
Streptomyces fradiae (Streptomyces roseoflavus).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1906;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W.,
Welzel K., Vente A.;
"Analysis and comparison of biosynthetic gene clusters for the 2-
deoxy-inosamine containing aminoglycoside antibiotics ribostamycin,
neomycin, lividomycin, paromomycin and butirosin.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
Subba B., Kharel M.K., Sthapit B., Liou K., Lee H.C., Woo J.S.,
Sohng J.K.;
"Cloning and characterization of a neomycin biosynthetic gene cluster
from Streptomyces fradiae, ATCC 10745.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
PubMed=16506694; DOI=10.1038/ja.2005.104;
Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., Kakinuma K.;
"Biosynthesis of 2-deoxystreptamine by three crucial enzymes in
Streptomyces fradiae NBRC 12773.";
J. Antibiot. 58:766-774(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND COFACTOR.
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
PubMed=15827636; DOI=10.1039/b501199j;
Huang F., Haydock S.F., Mironenko T., Spiteller D., Li Y.,
Spencer J.B.;
"The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB
8233: characterisation of an aminotransferase involved in the
formation of 2-deoxystreptamine.";
Org. Biomol. Chem. 3:1410-1418(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-257.
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150, and
ATCC 21096 / DSM 40943 / NBRC 13147 / MA-2898 / NRRL B-3357;
PubMed=12546424;
Tamegai H., Eguchi T., Kakinuma K.;
"First identification of Streptomyces genes involved in the
biosynthesis of 2-deoxystreptamine-containing aminoglycoside
antibiotics. Genetic and evolutionary analysis of L-glutamine:2-deoxy-
scyllo-inosose aminotransferase genes.";
J. Antibiot. 55:1016-1018(2002).
-!- FUNCTION: Catalyzes the PLP-dependent transamination of 2-deoxy-
scyllo-inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA)
using L-glutamine as the amino donor. Also catalyzes the
transamination of 3-amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA)
into 2-deoxystreptamine (2-DOS). {ECO:0000269|PubMed:16506694}.
-!- CATALYTIC ACTIVITY: L-glutamine + 2-deoxy-scyllo-inosose = 2-
oxoglutaramate + 2-deoxy-scyllo-inosamine.
{ECO:0000250|UniProtKB:Q6L739}.
-!- CATALYTIC ACTIVITY: L-glutamine + 3-amino-2,3-dideoxy-scyllo-
inosose = 2-oxoglutaramate + 2-deoxystreptamine.
{ECO:0000250|UniProtKB:Q6L739}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:15827636};
-!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step
2/4.
-!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step
4/4.
-!- PATHWAY: Antibiotic biosynthesis; neomycin biosynthesis.
-!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. L-glutamine:2-
deoxy-scyllo-inosose/scyllo-inosose aminotransferase subfamily.
{ECO:0000305}.
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EMBL; AJ629247; CAF33311.1; -; Genomic_DNA.
EMBL; AJ786317; CAH05102.1; -; Genomic_DNA.
EMBL; AB211959; BAD95819.1; -; Genomic_DNA.
EMBL; AJ843080; CAH58689.1; -; Genomic_DNA.
EMBL; AB066368; BAD30055.1; -; Genomic_DNA.
EMBL; AB066369; BAD30056.1; -; Genomic_DNA.
ProteinModelPortal; Q53U20; -.
SMR; Q53U20; -.
KEGG; ag:BAD95819; -.
KO; K13547; -.
BioCyc; MetaCyc:MONOMER-17227; -.
BRENDA; 2.6.1.100; 5932.
BRENDA; 2.6.1.101; 5932.
BRENDA; 2.6.1.50; 5932.
UniPathway; UPA00907; UER00922.
UniPathway; UPA00907; UER00924.
UniPathway; UPA00969; -.
GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
CDD; cd00616; AHBA_syn; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR000653; DegT/StrS_aminotransferase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PANTHER; PTHR30244; PTHR30244; 1.
Pfam; PF01041; DegT_DnrJ_EryC1; 1.
PIRSF; PIRSF000390; PLP_StrS; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
Transferase.
CHAIN 1 424 L-glutamine:2-deoxy-scyllo-inosose
aminotransferase.
/FTId=PRO_0000233015.
MOD_RES 202 202 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
SEQUENCE 424 AA; 44788 MW; 025849729266BA3C CRC64;
MVSPLAVKGG EALRTRPWPA WPQPAPGVPA AVAEVLGSGR WSISGPYRGT DSHERRFARA
FADYHGVPYC VPAASGTAGL MLALEACGVG AGDEVIVPGL SWVASGSTVL GVNAVPVFCD
VDPDTLCVSP EAVEALITER TRAVVVVHLY SAVADMDGLT RVAERHGLPL VEDCAQAHGA
SYRGVKVGAL ATAGTFSMQH SKVLTSGEGG AVITRDADLA RRVEHLRADG RCLSDGPPAP
GAMELVETGE LMGSNRCLSE FQAAILTEQL TLLDEQNRTR RANAARLDGL LGELGLRPQA
TSEGTTSRTY YTYAARLPEG ALEDVPLTDV TGALTAELGF PVQPCYAPIP ANRLYAPQTR
RRYTLGPDHE ARIDPKRFAL PVCEDTARRT VTLHHAALLG DAEDMADIAA AFAKVLRHGA
DLAT


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