GenomeNet

Database: UniProt
Entry: L0EG17_THECK
LinkDB: L0EG17_THECK
Original site: L0EG17_THECK 
ID   L0EG17_THECK            Unreviewed;       392 AA.
AC   L0EG17;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Putative PLP-dependent enzyme possibly involved in cell wall biogenesis {ECO:0000313|EMBL:AGA59218.1};
GN   OrderedLocusNames=Theco_3162 {ECO:0000313|EMBL:AGA59218.1};
OS   Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX   NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA59218.1, ECO:0000313|Proteomes:UP000010795};
RN   [1] {ECO:0000313|Proteomes:UP000010795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18247 / JCM 13945 / KWC4
RC   {ECO:0000313|Proteomes:UP000010795};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL   Submitted (JAN-2012) 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   ---------------------------------------------------------------------------
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; CP003255; AGA59218.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0EG17; -.
DR   STRING; 717605.Theco_3162; -.
DR   KEGG; tco:Theco_3162; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_2_1_9; -.
DR   Proteomes; UP000010795; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010795}.
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   392 AA;  42129 MW;  41BC45D6FB9CDE16 CRC64;
     MKTTVPKAAI LLSPPHMSGA EQHYIAEAFA SNWIAPLGPH VDAFERELAE AVGAGHAAAV
     SSGTAAIHLA LRLLGVGPGD RVFCSSLTFV ASANPILYQG AEPVFIDAEP ETWGMSPQAL
     ERALDEAAKE GRLPKAVIVV HLFGQCARMD EISALCGTYG VPIVEDAAEA LGSSYKGRHA
     GTIGRFGIYS FNGNKIITTS GGGMLVSDDG DAIREARVLA SQARDPAVHY EHSRPGYNYR
     LSNVLAGIGR AQLKVLADRV EARRAIFERY RTALEARPGI RFMPELPGTR SNRWLTALTV
     DEHLAGVTAS QLVAWLAEDR IESRPVWKPL HLQPLFAGAR FYSHGIREDV SARLFRTGIC
     LPSGSAMTPE EQERVIERLK AGMKSGQAAA GT
//
DBGET integrated database retrieval system