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Database: UniProt
Entry: A0A101UG63_9ACTN
LinkDB: A0A101UG63_9ACTN
Original site: A0A101UG63_9ACTN 
ID   A0A101UG63_9ACTN        Unreviewed;       399 AA.
AC   A0A101UG63;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0000313|EMBL:KUO10103.1};
GN   ORFNames=AQJ58_21900 {ECO:0000313|EMBL:KUO10103.1};
OS   Streptomyces sp. DSM 15324.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO10103.1, ECO:0000313|Proteomes:UP000053431};
RN   [1] {ECO:0000313|EMBL:KUO10103.1, ECO:0000313|Proteomes:UP000053431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO10103.1,
RC   ECO:0000313|Proteomes:UP000053431};
RA   Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUO10103.1}.
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DR   EMBL; LMXA01000019; KUO10103.1; -; Genomic_DNA.
DR   RefSeq; WP_067252513.1; NZ_KQ949028.1.
DR   AlphaFoldDB; A0A101UG63; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000053431; Unassembled WGS sequence.
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; 3.90.1150.10; 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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KUO10103.1};
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053431};
KW   Transferase {ECO:0000313|EMBL:KUO10103.1}.
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   399 AA;  42118 MW;  C278144F21E68231 CRC64;
     MSDGPGMRYE TWRALALWGE EEEAAALEVI RSRSPFRYYG PDLAHRTDAF EAAFSAATGV
     AHTVAVSSGT AALTAALIGL GIPAGAEVIV PGVTFVASVG AVVGARGIPV FAEVDDSLTL
     DPARLEERIT GRTWGVMPVH LHHAAADMDP ITEVARRHGL RVVEDAAQAA GVRYRGRPVG
     GLGDAGAFSF QLDKNITAGE GGAVTTSDAD VRDRVARYQD QGGQFTTAKG ATRGTADAPP
     FIGTNLRMTE LAAAVLGAQL PRLLPMCRRL RDVARRVRAE TADLPVRWRR LPDEEGSGGD
     LTLFVGSRLQ ARAVVADLHA AGIPAHTLYQ GQPVTANRAV REGRTPWGVE WERPPRLRTS
     EALLGRSVTI ALGAAMTDED VDAVVAAVRK ACQGIDAAG
//
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