GLDSA_STRFR
ID GLDSA_STRFR Reviewed; 424 AA.
AC Q53U20; Q6F6I2;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, 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:0000250|UniProtKB:Q6L739};
DE AltName: Full=Bifunctional L-glutamine:ketocyclitol aminotransferase I/II;
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:0000250|UniProtKB:Q6L739};
GN Name=neoB; Synonyms=nemB, neo6, neoS, nmcS;
OS Streptomyces fradiae (Streptomyces roseoflavus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1906;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W.,
RA Welzel K., Vente A.;
RT "Analysis and comparison of biosynthetic gene clusters for the 2-deoxy-
RT inosamine containing aminoglycoside antibiotics ribostamycin, neomycin,
RT lividomycin, paromomycin and butirosin.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RA Subba B., Kharel M.K., Sthapit B., Liou K., Lee H.C., Woo J.S., Sohng J.K.;
RT "Cloning and characterization of a neomycin biosynthetic gene cluster from
RT Streptomyces fradiae, ATCC 10745.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RX PubMed=16506694; DOI=10.1038/ja.2005.104;
RA Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., Kakinuma K.;
RT "Biosynthesis of 2-deoxystreptamine by three crucial enzymes in
RT Streptomyces fradiae NBRC 12773.";
RL J. Antibiot. 58:766-774(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND COFACTOR.
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RX PubMed=15827636; DOI=10.1039/b501199j;
RA Huang F., Haydock S.F., Mironenko T., Spiteller D., Li Y., Spencer J.B.;
RT "The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233:
RT characterisation of an aminotransferase involved in the formation of 2-
RT deoxystreptamine.";
RL Org. Biomol. Chem. 3:1410-1418(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-257.
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150, and
RC ATCC 21096 / DSM 40943 / NBRC 13147 / MA-2898 / NRRL B-3357;
RX PubMed=12546424; DOI=10.7164/antibiotics.55.1016;
RA Tamegai H., Eguchi T., Kakinuma K.;
RT "First identification of Streptomyces genes involved in the biosynthesis of
RT 2-deoxystreptamine-containing aminoglycoside antibiotics. Genetic and
RT evolutionary analysis of L-glutamine:2-deoxy-scyllo-inosose
RT aminotransferase genes.";
RL J. Antibiot. 55:1016-1018(2002).
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:16506694}.
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:0000250|UniProtKB:Q6L739};
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:0000250|UniProtKB:Q6L739};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15827636};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 2/4.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 4/4.
CC -!- PATHWAY: Antibiotic biosynthesis; neomycin biosynthesis.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. L-glutamine:2-deoxy-
CC scyllo-inosose/scyllo-inosose aminotransferase subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ629247; CAF33311.1; -; Genomic_DNA.
DR EMBL; AJ786317; CAH05102.1; -; Genomic_DNA.
DR EMBL; AB211959; BAD95819.1; -; Genomic_DNA.
DR EMBL; AJ843080; CAH58689.1; -; Genomic_DNA.
DR EMBL; AB066368; BAD30055.1; -; Genomic_DNA.
DR EMBL; AB066369; BAD30056.1; -; Genomic_DNA.
DR AlphaFoldDB; Q53U20; -.
DR SMR; Q53U20; -.
DR KEGG; ag:BAD95819; -.
DR BioCyc; MetaCyc:MON-17227; -.
DR BRENDA; 2.6.1.100; 5932.
DR BRENDA; 2.6.1.101; 5932.
DR BRENDA; 2.6.1.50; 5932.
DR UniPathway; UPA00907; UER00922.
DR UniPathway; UPA00907; UER00924.
DR UniPathway; UPA00969; -.
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 PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..424
FT /note="L-glutamine:2-deoxy-scyllo-inosose aminotransferase"
FT /id="PRO_0000233015"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ 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
