ID A0A075RHE9_BRELA Unreviewed; 372 AA.
AC A0A075RHE9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase {ECO:0000313|EMBL:AIG28630.1};
DE EC=2.6.1.90 {ECO:0000313|EMBL:AIG28630.1};
GN ORFNames=BRLA_c043660 {ECO:0000313|EMBL:AIG28630.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG28630.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG28630.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG28630.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP007806; AIG28630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075RHE9; -.
DR STRING; 1042163.BRLA_c043660; -.
DR KEGG; blr:BRLA_c043660; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_9; -.
DR Proteomes; UP000005850; 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:AIG28630.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000005850};
KW Transferase {ECO:0000313|EMBL:AIG28630.1}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 372 AA; 41523 MW; 0A0A6EBA44742368 CRC64;
MNVRIPIIDL TDEVELLWNE INSAVQEVLR SGHFVLGNEG KTFEKEVADY LGCKHAITVN
SGTDALFIAL RALEIGAGDE VIVPSFTFYA TAEAVELVGA TPVFAEINPD TFNVEPADIE
SKITERTRAI IPVHLYGHAA KMEPMITIAQ QYGLGLIEDT AQAFGGEYCG KKLGTFGHFG
CFSFYPTKNL GAYGDGGMLT TDNDELAEIA RKLRTHGSLI PYQNELTGYN SRLDELQACI
LRVKLPYINQ WNEARREAAQ QYNQMLKDVP GIVTPKVAGY AKHVYHQYTI RVKHGLRDEL
HRYLHQQGIG AMLYYPTPVH QLPVYQATQQ PKLAVTEQMA TEALSLPMWP RITLEIQQRV
VHAIQSFMAK VG
//
