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Database: UniProt
Entry: C9Y034_CROTZ
LinkDB: C9Y034_CROTZ
Original site: C9Y034_CROTZ 
ID   C9Y034_CROTZ            Unreviewed;       335 AA.
AC   C9Y034;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:CBA29572.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:CBA29572.1};
GN   Name=ltaE {ECO:0000313|EMBL:CBA29572.1};
GN   OrderedLocusNames=Ctu_14810 {ECO:0000313|EMBL:CBA29572.1};
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA29572.1, ECO:0000313|Proteomes:UP000002069};
RN   [1] {ECO:0000313|Proteomes:UP000002069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC   {ECO:0000313|Proteomes:UP000002069};
RX   PubMed=21037008; DOI=10.1128/JB.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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DR   EMBL; FN543093; CBA29572.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9Y034; -.
DR   KEGG; ctu:CTU_14810; -.
DR   PATRIC; fig|693216.3.peg.1412; -.
DR   HOGENOM; CLU_029381_0_3_6; -.
DR   OMA; MIDFRSD; -.
DR   Proteomes; UP000002069; Chromosome.
DR   GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_like; 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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CBA29572.1}.
FT   DOMAIN          3..282
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   335 AA;  36461 MW;  950D4D75EB812E6D CRC64;
     MIDLRSDTVT RPGKAMLERM MAAPTGDDVY GDDPTVNALQ DYAARLSGKE AALFLPTGTQ
     ANLVALLSHC ERGEEYIVGQ LAHNYLYEAG GAAVLGSIQP QPIEANGDGT LPLDKVAAKI
     KPDDVHFART RLLSLENTHN GKVLPRDYLQ QAWNFTRERG LALHVDGARI FNAVVAYGCE
     LKDIAQYCDT FTICLSKGLG APVGSLLLGS HDYIKRATRW RKMTGGGMRQ AGILAAAGLY
     ALEHNVARLQ EDHDNAAWLA AALRDAGADV RRHDTNMLFI SVPPAQVAAL GAFMKSRDVL
     ISAAPVTRLV MHLDVNRAQL ETLVAYWREF LQQAA
//
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