ID E1WQ59_BACF6 Unreviewed; 366 AA.
AC E1WQ59;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:CBW21645.1};
GN OrderedLocusNames=BF638R_1086 {ECO:0000313|EMBL:CBW21645.1};
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW21645.1, ECO:0000313|Proteomes:UP000008560};
RN [1] {ECO:0000313|EMBL:CBW21645.1, ECO:0000313|Proteomes:UP000008560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R {ECO:0000313|EMBL:CBW21645.1,
RC ECO:0000313|Proteomes:UP000008560};
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(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; FQ312004; CBW21645.1; -; Genomic_DNA.
DR RefSeq; WP_005795850.1; NC_016776.1.
DR AlphaFoldDB; E1WQ59; -.
DR KEGG; bfg:BF638R_1086; -.
DR PATRIC; fig|862962.3.peg.1106; -.
DR HOGENOM; CLU_033332_6_0_10; -.
DR Proteomes; UP000008560; Chromosome.
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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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:CBW21645.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:CBW21645.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 366 AA; 41219 MW; B7607897373188F8 CRC64;
MIKFLDLQKV TQRYSDEIQN SVARVVNSGW YLQGVENSSF EQKYSQYIGA KYTIGCANGL
DALIWIFRAY IELGLMQPGD EIIVPSNTYI ASILSITENG LIPVLVEPDI NTYQIDDKKI
EAAITNRTKA ILIVHLYGQC AYTEKISTIC KKFDLKLVED NAQAHGCIWG NQKTGSLGNA
AAHSFYPGKN LGALGDGGAV TTDDEELANV VRALANYGST KKYVFQYTGR NSRLDEIQAA
VLNVKLKYLD KDNGYRKKIA RYYIDNITNS QIILPKVSDW NAHVFHIFPV RCKKRNELQS
YLAENGIQTI IHYPIPPHKQ ECYKAWNNLS FPVSEIIHKE ELSLPISPVL TDVEAKKIVS
VINQFK
//
