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Database: UniProt
Entry: A0A257EQ58_9PROT
LinkDB: A0A257EQ58_9PROT
Original site: A0A257EQ58_9PROT 
ID   A0A257EQ58_9PROT        Unreviewed;       400 AA.
AC   A0A257EQ58;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=CFE37_06530 {ECO:0000313|EMBL:OYU15220.1};
OS   Alphaproteobacteria bacterium PA4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=2015572 {ECO:0000313|EMBL:OYU15220.1, ECO:0000313|Proteomes:UP000215773};
RN   [1] {ECO:0000313|EMBL:OYU15220.1, ECO:0000313|Proteomes:UP000215773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA4 {ECO:0000313|EMBL:OYU15220.1};
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|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:OYU15220.1}.
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DR   EMBL; NKIQ01000011; OYU15220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257EQ58; -.
DR   Proteomes; UP000215773; 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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42832:SF1; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAC; 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:OYU15220.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215773};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:OYU15220.1}.
FT   DOMAIN          32..383
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   400 AA;  43431 MW;  A3E948EDC36E772F CRC64;
     MTEDFYRIKR LPPYVIAEVN AMRAAARARG DDIIDLGMGN PDLPPPPHVI DKLCEVARKP
     DAHGYSASKG IPGLRKAQAG YYGRRFGVDV DPDSEVVVTL GSKEGLANLA QAITAPGDVV
     LAPNPSYPIH TFGFIIAGAT IRSVPTTPDE RYFEALERAM RFTVPKPSVL VMGYPSNPTA
     ETVDLAFYER VVAFAKKHQL WVLSDLAYSE LYYDGNPTPS ILQVQGAKDV AIEFTSLSKT
     YSMAGWRIGF AVGNKTLIGA LTRVKSYLDY GAFTPIQAAA VAAINGPQDI VADNRNLYHR
     RRDVLVESFG RAGWEIPSPR ASMFCWAPLP PALAHLGSLE FSKQLLTQAG VAVAPGVGYG
     EDGEGFVRIA MVENEQRLRQ AARNVKKYLT SMGVNTPGKG
//
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