ID L1L2B5_9ACTN Unreviewed; 439 AA.
AC L1L2B5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:EKX66820.1};
GN ORFNames=STRIP9103_05365 {ECO:0000313|EMBL:EKX66820.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX66820.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX66820.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX66820.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:EKX66820.1}.
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DR EMBL; AEJC01000191; EKX66820.1; -; Genomic_DNA.
DR AlphaFoldDB; L1L2B5; -.
DR PATRIC; fig|698759.3.peg.2635; -.
DR Proteomes; UP000010411; 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:UniProt.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EKX66820.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW Transferase {ECO:0000313|EMBL:EKX66820.1}.
SQ SEQUENCE 439 AA; 47252 MW; C0FEAE22DE13F042 CRC64;
MKAADRAHVF HSWSAQELID PLPVAGAEGS YFWDYDGNRY LDFTSGLVFT NIGYQHPKVV
AAIQEQAATM TTFAPAFAVE ARSEAARLIA ERTPGDLDKI FFTNGGADAV EHAVRMARLH
TGRPKVLAAY RSYHGGTQQA VNITGDPRRW ASDTAAAGVV HFWAPFLYRS RFYAETEEQE
CARALEHLET TIAFEGPSTI AAIILETIPG TAGIMIPPPG YLAGVRDLCD KYGIVFVLDE
VMAGFGRTGK WFAADHFDVV PDLMTFAKGV NSGYVPLGGV AISGTIAETF ARRPYPGGLT
YSGHPLACGA AVATINVMAE EGIVDNAAEL GATLIEPALR ELAARHPSVG EVRGVGMFWA
LELVKNKETR EPLVPYNATG EANTPMLAFA KAARSQGLWP FVNMNRTHVV PPCNITESEA
KEGLAALDAA LTVADEYTV
//
