ID J1ZS05_9ACTN Unreviewed; 398 AA.
AC J1ZS05;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=SU9_24212 {ECO:0000313|EMBL:EJJ04361.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ04361.1};
RN [1] {ECO:0000313|EMBL:EJJ04361.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ04361.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
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:EJJ04361.1}.
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DR EMBL; AJGV01000147; EJJ04361.1; -; Genomic_DNA.
DR AlphaFoldDB; J1ZS05; -.
DR STRING; 1160718.SU9_24212; -.
DR PATRIC; fig|1160718.3.peg.4898; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_2_11; -.
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 Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 72..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 41425 MW; 5AD22250CCBBDEE9 CRC64;
MRVPGGGGGR PGDRRRDAAD RFSGGGHRGA VTVPARTGSA RLPAPPAAPP PEPDLRHHGD
AEVRGADGAL TDLAVNVRTG TPPAWLKARI AASLDTLAAY PDGRAARRAV AARHGLPVER
VLLTSGAAEA FVLLARAVRA RRPVVVHPQF TEPEAALRDA GHEVGRVLLD ARDGFRLDPA
AVPEDADLVV VGNPTNPTSV LHPADVLARL ARPGRTLVVD EAFMDAVPGE REALAGRTDL
PGLVVLRSLT KTWGLAGLRI GYVLADPDTV AALERAQPLW PVSSPALAAA EACSAPGALA
EAAAAAGQIA ADRDHLLARL AAFGQIRTVA PAAGPFVLLR LPGADEVRAA LRTRGFAVRR
GDTFPGLGPD WLRLAVRDRA TTDRFAAALD DVLDEALT
//
