ID A0A087MJX7_9GAMM Unreviewed; 500 AA.
AC A0A087MJX7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Lysine 6-aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N788_10865 {ECO:0000313|EMBL:KFL37180.1};
OS Arenimonas donghaensis DSM 18148 = HO3-R19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121014 {ECO:0000313|EMBL:KFL37180.1, ECO:0000313|Proteomes:UP000029085};
RN [1] {ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|Proteomes:UP000029085};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas donghaensis.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFL37180.1, ECO:0000313|Proteomes:UP000029085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO3-R19 {ECO:0000313|EMBL:KFL37180.1,
RC ECO:0000313|Proteomes:UP000029085};
RX PubMed=26380644; DOI=10.1186/s40793-015-0055-4;
RA Chen F., Wang H., Cao Y., Li X., Wang G.;
RT "High quality draft genomic sequence of Arenimonas donghaensis DSM
RT 18148(T).";
RL Stand. Genomic Sci. 10:59-59(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {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:KFL37180.1}.
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DR EMBL; AVCJ01000006; KFL37180.1; -; Genomic_DNA.
DR RefSeq; WP_034221656.1; NZ_AVCJ01000006.1.
DR AlphaFoldDB; A0A087MJX7; -.
DR STRING; 1121014.N788_10865; -.
DR PATRIC; fig|1121014.3.peg.928; -.
DR OrthoDB; 6188639at2; -.
DR Proteomes; UP000029085; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF112; PUTRESCINE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000029085};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 500 AA; 53990 MW; 690FE8FB66C8E09F CRC64;
MNLLEILKPL RSRAGTVRTP GLDDASLQRL GARFPELVEA AKAAAEAHAA LATEFADLFD
LDEQAQVEAV QAGFVNFYPD DAVNPYVALA ARGPWIVTLK GAVIHDSGGY GMLGLGHTPA
PLLEAMSRPQ VMANVMTPSL SQLRIVRALR KEIGHRRDEC PYAKFLCLNS GSESVSLAGR
IADVNAKLHT DAGGRHAGKR VKRVAVKGAF HGRTELPALY SDSSRKNYLQ HLASYQHHND
QLLVVEPYSV EGLKQVFADA DANGWYIEAM FLEPVMGEGD PGRAVPPEFY AAARELTKAH
GTLLLVDSIQ AGLRAHGVLS IVDYPGFEGL EAPDMETYSK ALNGGQYPLS VLAVNERAAG
LYRKGVYGNT MTANPRALDI AAAMLGQLTP ELRANIRDRG QEFLDKLAAL RDELGNGLIT
KVQGTGLLFS CELDPSFKCF GAGSTEEYMR ERGIGVIHGG TNSLRFTPHF AVTSEEVDLV
IDNIRQALLH GPRKTQAAAA
//
