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
//