ID B6EPC8_ALISL Unreviewed; 381 AA.
AC B6EPC8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:CAQ77856.1};
GN OrderedLocusNames=VSAL_I0171 {ECO:0000313|EMBL:CAQ77856.1}, VSAL_I0252
GN {ECO:0000313|EMBL:CAQ77937.1};
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ77856.1, ECO:0000313|Proteomes:UP000001730};
RN [1] {ECO:0000313|EMBL:CAQ77856.1, ECO:0000313|Proteomes:UP000001730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ77856.1,
RC ECO:0000313|Proteomes:UP000001730};
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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}.
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DR EMBL; FM178379; CAQ77856.1; -; Genomic_DNA.
DR EMBL; FM178379; CAQ77937.1; -; Genomic_DNA.
DR RefSeq; WP_012549053.1; NC_011312.1.
DR AlphaFoldDB; B6EPC8; -.
DR KEGG; vsa:VSAL_I0171; -.
DR KEGG; vsa:VSAL_I0252; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_6; -.
DR Proteomes; UP000001730; Chromosome 1.
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; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
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:CAQ77856.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:CAQ77856.1}.
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 381 AA; 42182 MW; 407CE601049CC0EE CRC64;
MNKTPLVEFV RDIYQTNDFI PLHAPTFDGN EQKYVLETIQ STFVSSVGKF VDEFEQKIES
YTGTAKAVAT VNGTAALHAA LYMAGVQHGD FVITQALTFV ATCNALHHMG AEPIFVDVSP
VSLGLCPKAM DEYLTQHAQV TETGCIHSQT KRPIRAVVPM HTFGHPVELD ELIAVCHKWN
ITLVEDAAES LGSFYKGKHT GTLGDFGAVS FNGNKIITTG GGGMVLCKTA ELGARTKHVT
TTAKVPHPYE FYHDEAGFNY RMPNLNAALG CAQMEVLEPY LAQKRVLANR YQDFFAESDF
QFVSEPEYAQ SNYWLNAVIC PSVDARNDIL KQTNESGVMT RPIWQLMHRL PMFKEAPRGD
LTQSEYIEAH LINLPSTPVA L
//
