ID   E3BCY1_9MICO            Unreviewed;       429 AA.
AC   E3BCY1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:EFP57094.1};
GN   ORFNames=HMPREF0321_0851 {ECO:0000313|EMBL:EFP57094.1};
OS   Dermacoccus sp. Ellin185.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=188626 {ECO:0000313|EMBL:EFP57094.1, ECO:0000313|Proteomes:UP000003057};
RN   [1] {ECO:0000313|EMBL:EFP57094.1, ECO:0000313|Proteomes:UP000003057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin185 {ECO:0000313|EMBL:EFP57094.1,
RC   ECO:0000313|Proteomes:UP000003057};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFP57094.1}.
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; AEIQ01000107; EFP57094.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3BCY1; -.
DR   eggNOG; COG0160; Bacteria.
DR   Proteomes; UP000003057; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:EFP57094.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EFP57094.1}.
SQ   SEQUENCE   429 AA;  45882 MW;  51924E57BAAEC56C CRC64;
     MTPDETYALD RAHVFHSWSA QAALKPMVVT KTSGSRLWDG DGNEYLDFTG QLVYTNVGHQ
     HPRVVEAIKT QAETLCTIGP SNANDQRSQL AKMISDLLPD TLNKVFFTNG GTEANEHAVR
     MAREVTGRRK LLAAYRSYHG ATAQSIHLTG EARRFANDKG ASEVVHFFGP FLYRSEFWAT
     SEDEECERAL THLEHTITSE GADAFAALIL EPVIGSAGII PPPPGYLEGV REICTKYGII
     FIADEVMAGF GRTGAWFAHQ HANVVPDLIT FAKGVNSGYV PLGGVVLSDE IAHHFDERAY
     PGGLTYSGHP LACAAGVATI AAMQDEGIVE NAARIGSDVL GPGLQALAEK HDAVGQARGV
     GVFWALELVE DAARTPDVER AAAVAAACKK TGLLVIAAAN RLHVVPPCNV SDDDVRAALT
     ILDEALSAS
//