ID   A0A1E5XEC6_9PSED        Unreviewed;       393 AA.
AC   A0A1E5XEC6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=AX279_01510 {ECO:0000313|EMBL:OEO26989.1};
OS   Pseudomonas sp. J237.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1904754 {ECO:0000313|EMBL:OEO26989.1, ECO:0000313|Proteomes:UP000095383};
RN   [1] {ECO:0000313|EMBL:OEO26989.1, ECO:0000313|Proteomes:UP000095383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J237 {ECO:0000313|EMBL:OEO26989.1,
RC   ECO:0000313|Proteomes:UP000095383};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) 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:OEO26989.1}.
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DR   EMBL; MKEP01000004; OEO26989.1; -; Genomic_DNA.
DR   RefSeq; WP_069897936.1; NZ_MKEP01000004.1.
DR   AlphaFoldDB; A0A1E5XEC6; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000095383; 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; 3.40.640.10; 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   PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR   PANTHER; PTHR46383; 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:OEO26989.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:OEO26989.1}.
FT   DOMAIN          33..381
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   393 AA;  43422 MW;  FF879DB7FDD40A14 CRC64;
     MAQPYSARSR AIEPFHVMAL LARANQLQID GHDVIHLEIG EPDFTTASPI IAAGQAALAE
     GHTRYTSARG IPALREAISG FYAQRYQLNI DPERILITPG GSGALLLATS LLVDPGKHWL
     LADPGYPCNR HFLRLIEGAA QLVPVGPDVR YQLTPELVER YWDKDSVGAL VASPANPTGT
     LLSADELAGL SQALKRRGGH LVVDEIYHGL TYGVDAHSVL EVDDEAFVLN SFSKYFGMTG
     WRLGWLVAPP AAVPELEKLA QNLYISAPSM AQQAALACFE PQTLEILEQR REEFARRRDF
     LLPALRELGF KIAVEPEGAF YLYADISAFG GDAFAFCKHF IETEYVAFTP GNDFGRFQAH
     QHVRFAYTQS LERLQQAVER IARGLKTWNP HAL
//