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 27-MAR-2024, entry version 87. 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; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; 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 / RC NRRL 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}. 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; 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; FIASSFC; -. DR OrthoDB; 9804264at2; -. DR BioCyc; MetaCyc:MONOMER-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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1. DR PANTHER; PTHR30244; TRANSAMINASE; 1. DR Pfam; PF01041; DegT_DnrJ_EryC1; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 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 //