GLDSA_STRRI
ID GLDSA_STRRI Reviewed; 424 AA.
AC Q4R0W2; Q6F6I0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 54.
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=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=rbmB; Synonyms=rbcS, ribS;
OS Streptomyces ribosidificus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=80859;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21294 / JCM 4923 / NBRC 13796 / NRRL B-11466;
RX PubMed=16258246;
RA Subba B., Kharel M.K., Lee H.C., Liou K., Kim B.-G., Sohng J.K.;
RT "The ribostamycin biosynthetic gene cluster in Streptomyces ribosidificus:
RT comparison with butirosin biosynthesis.";
RL Mol. Cells 20:90-96(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21294 / JCM 4923 / NBRC 13796 / NRRL B-11466;
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-257.
RC STRAIN=ATCC 21294 / JCM 4923 / NBRC 13796 / NRRL B-11466;
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:0000250|UniProtKB:Q6L739}.
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:0000250};
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; ribostamycin 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; AJ748131; CAG34719.1; -; Genomic_DNA.
DR EMBL; AJ744850; CAG34038.1; -; Genomic_DNA.
DR EMBL; AB066371; BAD30058.1; -; Genomic_DNA.
DR PDB; 5W70; X-ray; 2.10 A; A/B=1-424.
DR PDBsum; 5W70; -.
DR AlphaFoldDB; Q4R0W2; -.
DR SMR; Q4R0W2; -.
DR BRENDA; 2.6.1.100; 6083.
DR BRENDA; 2.6.1.50; 6083.
DR UniPathway; UPA00907; UER00922.
DR UniPathway; UPA00907; UER00924.
DR UniPathway; UPA00972; -.
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 3D-structure; Aminotransferase; Antibiotic biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..424
FT /note="L-glutamine:2-deoxy-scyllo-inosose aminotransferase"
FT /id="PRO_0000233021"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 228
FT /note="A -> V (in Ref. 3; BAD30058)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5W70"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5W70"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 273..293
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:5W70"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:5W70"
FT HELIX 402..416
FT /evidence="ECO:0007829|PDB:5W70"
SQ SEQUENCE 424 AA; 45012 MW; 14C6CF9ED12792C6 CRC64;
MVSQLAVKGG EALRTRPWPA WPQPAPGVPD AVADVLGSGR WSISGPYRGT ESYERRFARA
FAAYNGVPHC VPAASGTASL MLALEACGIG AGDEVIVPGL SWVASGSTIL GVNAVPIFCD
VDPDTLCLSP EAVEAAITEH TRAIVVVHLY SALADMDALS AIAERHGLPL IEDCAQAHGA
TYRGVKVGAL ATAGTFSMQH SKVLTSGEGG AVITRDEDFA RRVEHLRADG RCLSAVPPAP
GAMELVETGE LMGNNRCLSE FQAAILAEQL TILDEQNETR RANAAHLDGL LGELGLRPQT
TSDGTTSRTY YTYAVRLPDG VLEDVPVTDV SCALTAELGF PVLPSYAPIP ANRLYTPHTR
RRYTLGLDHE RRIDPKRFAL PVCEDAARRT VTLHHAALLG DADDMGDIAA AFAKVLRHGA
GLMH
