ID   GLSA_STRGR              Reviewed;         424 AA.
AC   P77952; Q53IE1;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=L-glutamine:scyllo-inosose aminotransferase;
DE            EC=2.6.1.50;
DE   AltName: Full=Glutamine--scyllo-inositol transaminase;
GN   Name=stsC; ORFNames=SG7F10.11c;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CHARACTERIZATION, COFACTOR,
RP   AND SUBUNIT.
RC   STRAIN=N2-3-11;
RX   PubMed=9238101; DOI=10.1007/s002030050475;
RA   Ahlert J., Distler J., Mansouri K., Piepersberg W.;
RT   "Identification of stsC, the gene encoding the L-glutamine:scyllo-inosose
RT   aminotransferase from streptomycin-producing Streptomycetes.";
RL   Arch. Microbiol. 168:102-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23345 / DSM 40236 / JCM 4644 / NBRC 12875 / NCIMB 13023 / NRRL
RC   B-2682 / VKM Ac-800 / IMRU 3463;
RA   van der Geize R., Dijkhuizen L., Wellington E.M., Piepersberg W.;
RT   "Cloning and heterologous expression of the str/sts-gene cluster from a
RT   Streptomyces griseus DSM40236 PAC library: the cluster for streptomycin
RT   production lies in a highly conserved genomic area.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the PLP-dependent transamination of scyllo-inosose
CC       to form scyllo-inosamine. {ECO:0000269|PubMed:9238101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamine + scyllo-inosose = 1-amino-1-deoxy-scyllo-inositol
CC         + 2-oxoglutaramate; Xref=Rhea:RHEA:22920, ChEBI:CHEBI:16769,
CC         ChEBI:CHEBI:17811, ChEBI:CHEBI:57671, ChEBI:CHEBI:58359; EC=2.6.1.50;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:9238101};
CC   -!- PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9238101}.
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; Y08763; CAA70012.1; -; Genomic_DNA.
DR   EMBL; AJ862840; CAH94315.1; -; Genomic_DNA.
DR   RefSeq; WP_003970228.1; NZ_UAVD01000010.1.
DR   AlphaFoldDB; P77952; -.
DR   SMR; P77952; -.
DR   GeneID; 6212512; -.
DR   OMA; KVYENRD; -.
DR   BioCyc; MetaCyc:MON-14011; -.
DR   UniPathway; UPA00066; -.
DR   GO; GO:0047310; F:glutamine-scyllo-inositol transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
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..424
FT                   /note="L-glutamine:scyllo-inosose aminotransferase"
FT                   /id="PRO_0000233018"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  45501 MW;  AED73E61EA9B0E33 CRC64;
     MDSSLAISGG PRLSNREWPR WPQPGDRALK SLEDVLTSGR WTISCAYQGR DSYERQFASA
     FADYCGSAMC VPISTGTASL AIALEACGVG AGDEVIVPGL SWVASASAVL GINAVPVLVD
     VDPATYCLDP AATEAAITER TRAITVVHAY SAVADLDALL DIARRHGLPL IEDCAHAHGA
     GFRGRPVGAH GAAGVFSMQG SKLLTCGEGG ALVTDDADVA LRAEHLRADG RVVRREPVGV
     GEMELEETGR MMGSNACLSE FHAAVLLDQL ELLDGQNARR TRAADHLTDR LSELGMTAQA
     TAPGTTARAY YRYLVRLPDE VLAVAPVERF AHALTAELGF AVTQTHRPLN DNPLNRPSSR
     RRFATDARYL ERVDPSRFDL PAAKRAHESV VSFSHEVLLA PLDAIDDIAR AFRKVLDNVR
     EVSR