ID A0A101S7E1_9ACTN Unreviewed; 356 AA.
AC A0A101S7E1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=AQJ54_12315 {ECO:0000313|EMBL:KUN68695.1};
OS Streptomyces griseorubiginosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN68695.1, ECO:0000313|Proteomes:UP000054375};
RN [1] {ECO:0000313|EMBL:KUN68695.1, ECO:0000313|Proteomes:UP000054375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN68695.1,
RC ECO:0000313|Proteomes:UP000054375};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT strain for the species Streptomyces griseorubiginosus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|RuleBase:RU000481};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:KUN68695.1}.
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DR EMBL; LMWV01000006; KUN68695.1; -; Genomic_DNA.
DR RefSeq; WP_062236847.1; NZ_KQ948735.1.
DR AlphaFoldDB; A0A101S7E1; -.
DR Proteomes; UP000054375; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:KUN68695.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054375};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KUN68695.1}.
FT DOMAIN 26..347
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 356 AA; 38083 MW; F3CD33E116BD7AE6 CRC64;
MRTEPAGAHD LRHHGDAEVR DDGAKLTDLA VNVRADTPPA WLRERIAGSL AGLAAYPDGR
AARAAVAARH GVAVERVLLT AGAAEAFVLL ARALTVRHAV VVHPQFTEPE AALRDAGHRV
ERALLREEDG FRLDPAAVPE DADLVVVGNP TNPTSVLHPA ATIAELTRPG RTLVVDEAFL
DAVPGEREAL AGRTDVPGLV VLRSLTKTWG LAGLRIGYVL AAPETIAALE RAQPLWPVST
PALAAAQACM EPRALAEAAH AAHRVATDRA HLVAGLREFA PDGLRVVEPA EGPFVLVRLP
RATAVRRHLR DLGWAVRRGD TFPGLDEEWL RLAVRDRPTV NRFLQALDQA VTLAKG
//
