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Database: UniProt
Entry: A0A2B2C147_9BACI
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ID   A0A2B2C147_9BACI        Unreviewed;       349 AA.
AC   A0A2B2C147;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:PFP25905.1};
GN   ORFNames=COJ96_19330 {ECO:0000313|EMBL:PFP25905.1};
OS   Bacillus sp. AFS073361.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP25905.1, ECO:0000313|Proteomes:UP000223997};
RN   [1] {ECO:0000313|EMBL:PFP25905.1, ECO:0000313|Proteomes:UP000223997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS073361 {ECO:0000313|EMBL:PFP25905.1,
RC   ECO:0000313|Proteomes:UP000223997};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) 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 threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PFP25905.1}.
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DR   EMBL; NUZU01000037; PFP25905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B2C147; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000223997; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000223997}.
FT   DOMAIN          25..286
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   349 AA;  38936 MW;  C0E065995339CED3 CRC64;
     MYSFKNDYSE GAHPRILNAL IESNLVQDDG YGEDQFSRQA VELLKERMGE PDVDVHLLSG
     GTQTNLIAIS AFLRPHEAAM AASTGHILGH ETGAIEATGH KILSIEAENG KLTPSDVQVV
     LDGHPDEHMV KPKLVYISNS TEIGSIYTRN ELEQLSDFCK KNHLILYMDG ARLGSALCSE
     ENDLQLSDLP RLVDAFYIGG TKNGALLGEA LVICRESLKE DFRYHMKQKG ALLAKGRLLG
     IQFLELFRDN LFFELATHAN KMAATLREGI SKANIPFLTH SPSNQIFPIL PNEFITELEK
     NYGFHFWEKV DEEHAAIRLV TSWATKDEGI AAFLEDLKGI IEKINRKSK
//
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