ID A0A2S1Z2T8_9ACTN Unreviewed; 377 AA.
AC A0A2S1Z2T8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Aminotransferase class V-fold PLP-dependent enzyme {ECO:0000313|EMBL:GBQ00651.1};
DE SubName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0000313|EMBL:AWK10704.1};
GN ORFNames=DDQ41_19380 {ECO:0000313|EMBL:AWK10704.1}, SSP531S_20690
GN {ECO:0000313|EMBL:GBQ00651.1};
OS Streptomyces spongiicola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1690221 {ECO:0000313|EMBL:AWK10704.1, ECO:0000313|Proteomes:UP000245051};
RN [1] {ECO:0000313|EMBL:AWK10704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HNM0071 {ECO:0000313|EMBL:AWK10704.1};
RA Zhou S., Huang X.;
RT "Complete genome sequence of the Type Strain of Streptomyces spongiicola
RT HNM0071, the producer of staurosporine.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GBQ00651.1, ECO:0000313|Proteomes:UP000265354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=531S {ECO:0000313|EMBL:GBQ00651.1,
RC ECO:0000313|Proteomes:UP000265354};
RA Dohra H., Kodani S.;
RT "Whole Genome Shotgun Sequence of Streptomyces spongiicola strain 531S.";
RL Submitted (JUL-2018) 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 ---------------------------------------------------------------------------
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; CP029254; AWK10704.1; -; Genomic_DNA.
DR EMBL; BGZL01000004; GBQ00651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1Z2T8; -.
DR KEGG; sspo:DDQ41_19380; -.
DR OrthoDB; 5342089at2; -.
DR Proteomes; UP000245051; Chromosome.
DR Proteomes; UP000265354; 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: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 Aminotransferase {ECO:0000313|EMBL:AWK10704.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:AWK10704.1}.
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 377 AA; 40591 MW; 6EA8C4BCFA326B6C CRC64;
MPQRETPLPT VLEPRGRTFG EEERAAVLRV LDSAVLCGAF GREARALESE MAALYGRAEA
VSSSSGTAAL HIALAAAGVG PGDEVVTTPV SDFGTVAPVL AQGARVVFAD VRADDGNLDP
AAVEAAITPR TRAVVAVHLF GGAADVARLR EICDRHGILL VEDCAQAWLG EDEDGRLLGT
AGDIACFSLQ QYKHITAGDG GLCITDDPEL ARGMRLFMDK GWDRSEGRIH RTMGLNYRMT
ELVAAVARAQ LARVPEVVRL RRERAARFAA AVERLVPAPG VRLPSRRAGH AWWVMPLLVD
DNSRWAHGLQ DAGVPALRGY LERPLYANPA LSGHHPGPCP RAETLIDRTL LVLQWNEGYT
EDDVDRIART LGEVGAR
//
