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Database: UniProt
Entry: A0A257JF12_9BURK
LinkDB: A0A257JF12_9BURK
Original site: A0A257JF12_9BURK 
ID   A0A257JF12_9BURK        Unreviewed;       244 AA.
AC   A0A257JF12;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
DE   Flags: Fragment;
GN   ORFNames=CFE45_36760 {ECO:0000313|EMBL:OYU73643.1};
OS   Burkholderiales bacterium PBB5.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015567 {ECO:0000313|EMBL:OYU73643.1, ECO:0000313|Proteomes:UP000215735};
RN   [1] {ECO:0000313|EMBL:OYU73643.1, ECO:0000313|Proteomes:UP000215735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB5 {ECO:0000313|EMBL:OYU73643.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU73643.1}.
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DR   EMBL; NKII01002885; OYU73643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257JF12; -.
DR   Proteomes; UP000215735; 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:OYU73643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215735};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:OYU73643.1}.
FT   DOMAIN          4..242
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   NON_TER         244
FT                   /evidence="ECO:0000313|EMBL:OYU73643.1"
SQ   SEQUENCE   244 AA;  26122 MW;  A966A339C8C45169 CRC64;
     MLGARVVRVS LVPDATGAWR LDLDRLLAAV TPATRVLLVN APNNPTGWTL SRSEQQAVLD
     HCRRTGTWIV ADEVYERVWF GPGGCAPSFQ DITTPQDRVI VVHSFSKSFL MTGWRLGWLV
     LPRGQLDAVG KLIEFNSSCA PVFVQRGGLA ALAMADDFVP GLVARLQAGR DALQPALAAL
     PGVVAALPPG GMYVWFRAPG ADDSLAFAKR LVAEVGLGLA PGAAFGDEGE GWLRWCFASQ
     DTAR
//
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