ID A0A101TBJ6_9ACTN Unreviewed; 403 AA.
AC A0A101TBJ6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=AQJ64_00725 {ECO:0000313|EMBL:KUN89239.1};
OS Streptomyces griseoruber.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN89239.1, ECO:0000313|Proteomes:UP000052982};
RN [1] {ECO:0000313|EMBL:KUN89239.1, ECO:0000313|Proteomes:UP000052982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN89239.1,
RC ECO:0000313|Proteomes:UP000052982};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT for the species Streptomyces griseoruber.";
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|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC 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:KUN89239.1}.
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DR EMBL; LMWW01000001; KUN89239.1; -; Genomic_DNA.
DR RefSeq; WP_059202307.1; NZ_KQ948763.1.
DR AlphaFoldDB; A0A101TBJ6; -.
DR STRING; 1943.AQJ64_00725; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000052982; 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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 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:KUN89239.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KUN89239.1}.
FT DOMAIN 34..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 43245 MW; 7EB1458324B55111 CRC64;
MTTAARVRRI SPSPSVAAAQ RVRELKSQGL TIHDLTVGEP DFDTPAHVKA AAIRAIEAGE
TKYTSVNGTP ALRAAIIEKL RRRHGLEYTD GTITVGGGAK QVIFLALTAT LDEGDEVVIP
APYWVSYPDM VRANDGTPVV VDCPESDGFK LTPERLRPAL TDRTRWVVLN TPGNPTGSAY
TTAELRALAA VLLEHPHVRV LTDEIYDEIW YDDGASPSLA AVEPRLADRV FLTNGVSKTY
AMTGWRLGYG AGPADLVTAV NTLQSQISSC PSSISQAAAA AALGGPQDFV RESVEVYRAR
RDTTVKLIRE IPQLTCTTPS GGFYLLVNCR AAVGRLTPTG HRIQDDEDFA RHLLDSEQVA
VIHGSAYGAP GYFRISFATS TEVLTEACAR IAAACAALSE RPS
//
