ID A0A0N0TRJ4_9ACTN Unreviewed; 431 AA.
AC A0A0N0TRJ4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ADL06_22135 {ECO:0000313|EMBL:KOX23574.1};
OS Streptomyces sp. NRRL F-6491.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX23574.1, ECO:0000313|Proteomes:UP000037743};
RN [1] {ECO:0000313|EMBL:KOX23574.1, ECO:0000313|Proteomes:UP000037743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX23574.1,
RC ECO:0000313|Proteomes:UP000037743};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KOX23574.1}.
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DR EMBL; LGEE01000227; KOX23574.1; -; Genomic_DNA.
DR RefSeq; WP_053645786.1; NZ_LGEE01000227.1.
DR AlphaFoldDB; A0A0N0TRJ4; -.
DR PATRIC; fig|1519495.3.peg.4726; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000037743; Unassembled WGS sequence.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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 Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 431 AA; 45752 MW; 7FA8D616FD11492D CRC64;
MTERPQQLAM VGGPRAVPPG TAAPRWPVIT RDDEEAVARV LASGRLTATA EGEEEVPGLE
REWAAYTGTA HCAAVGSGTA ALQLALAALG VGPGDEVVVP SLSMNATALA VLQQGARPVF
ADVDPETYTM DPEAVRAVAG PRTKALLPVH LHGLPADMDA LRAVADGLGA AVVEDAAQSH
GASYRGRRTG ALGTVGCFSL HPSKNLPSCG EGGLLTTDDP ELYERVLRLR QFGEDPRPRH
TRSYVSHTPG WNHRIGPVEA AFARGQLTRL DAYGRRRTPG ILAFLDRLAA LPGLRVPVVP
EGSAHVWHIL RFRLDPEALG LAHGDAAALR RALHRALRAE GVPVSRYQEA PLPAHPAFAP
YVPAGADFPV AHAVLTDSLC LQRRQLDPDS GPVLAAYADG FEKVWRNLDL IRRMVRSASP
AGRERQGAGV A
//
