ID E0RYL2_BUTPB Unreviewed; 400 AA.
AC E0RYL2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Aminotransferase DegT/DnrJ/EryC1/StrS family {ECO:0000313|EMBL:ADL33093.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ADL33093.1};
GN OrderedLocusNames=bpr_I0345 {ECO:0000313|EMBL:ADL33093.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL33093.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL33093.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(2010).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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; CP001810; ADL33093.1; -; Genomic_DNA.
DR RefSeq; WP_013279750.1; NC_014387.1.
DR AlphaFoldDB; E0RYL2; -.
DR STRING; 515622.bpr_I0345; -.
DR KEGG; bpb:bpr_I0345; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_9; -.
DR Proteomes; UP000001299; 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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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:ADL33093.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000001299};
KW Transferase {ECO:0000313|EMBL:ADL33093.1}.
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 400 AA; 44880 MW; B6EA942023D82B64 CRC64;
MEKEKLAIHG GKPVRENKIF YGRQWIQDDD VQAIAAVLKG DYITCGPSVD AVEKKISEVT
GAKYTVVVAN GTAALHCAAI AAGLGEGDEV ITTPLTFAAS ANCAVYVGAR PVFADVNPET
YNIDPDSIEA HITDKTRAVV AVDFTGQAVE HDRIREICKK HNLVYICDAA HAIGTRYKGQ
PEGSIADMTC FSFHPVKTIT SGEGGAITTN DPELYKKLRL ASQHGIVRNP DDFVEKNPEG
IWYYEMQTLG YNYRMTDFQA ALLSSQLNKL EQFSNRRKEI VNKYNEAFKD VPEIIVQKEI
PESDTTRHLY IIQLDLDKLT CTRREFFDAM SAENVQCQVH YVPVYWFPFY QNMGYTKGLC
PNAEKIYKGI MSIPLYPMLT DEDVESSIAA VKKIVNWYRK
//
