ID A0A0A0ETP5_9GAMM Unreviewed; 369 AA.
AC A0A0A0ETP5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KGM53859.1};
GN ORFNames=N800_03655 {ECO:0000313|EMBL:KGM53859.1};
OS Lysobacter daejeonensis GH1-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385517 {ECO:0000313|EMBL:KGM53859.1, ECO:0000313|Proteomes:UP000029998};
RN [1] {ECO:0000313|EMBL:KGM53859.1, ECO:0000313|Proteomes:UP000029998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GH1-9 {ECO:0000313|EMBL:KGM53859.1,
RC ECO:0000313|Proteomes:UP000029998};
RA Zhang S., Wang G.;
RT "Genome sequencing of Lysobacter.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:KGM53859.1}.
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; AVPU01000020; KGM53859.1; -; Genomic_DNA.
DR RefSeq; WP_036138466.1; NZ_AVPU01000020.1.
DR AlphaFoldDB; A0A0A0ETP5; -.
DR STRING; 1385517.N800_03655; -.
DR eggNOG; COG0399; Bacteria.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000029998; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KGM53859.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000029998};
KW Transferase {ECO:0000313|EMBL:KGM53859.1}.
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 369 AA; 40945 MW; F25CD2C4E6788A51 CRC64;
MIPVNQPLLD GNEKKYLLEC IDTGWISSEG PFVKQFEDGF AARVRRRHGV AVCNGTAALD
AAIEALGIGP GDEVILPTFT IISCIIQIVR AGATPVLVDS DPATWNMDTD QIEAKISSRT
KAIMVVHTYG LPVDMDPVLD IARRYGLRVI EDAAEMHGQT YKGRPCGSFG DVSTFSFYPN
KHVTTGEGGM VLVDDDSLAD DCRSLRNLCF QPHKRFVHER LGWNLRMTNM QAALGLAQLE
RLDEFVARKR HIGARYSAGL ADLPSARLPL AGTHYADNIY WVFGLVIDEE KGMDAEDVMK
RLASEGVGTR PFFCPMHQQP VLRRMGLFEN DRHPVAELMY RQGFYLPSGM ALSDGDIDRT
IEAVWKVLG
//