ID K8B696_9ENTR Unreviewed; 335 AA.
AC K8B696;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:CCJ81885.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:CCJ81885.1};
GN ORFNames=BN134_2644 {ECO:0000313|EMBL:CCJ81885.1};
OS Cronobacter dublinensis 1210.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1208656 {ECO:0000313|EMBL:CCJ81885.1, ECO:0000313|Proteomes:UP000009342};
RN [1] {ECO:0000313|EMBL:CCJ81885.1, ECO:0000313|Proteomes:UP000009342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1210 {ECO:0000313|EMBL:CCJ81885.1,
RC ECO:0000313|Proteomes:UP000009342};
RX PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA McClelland M., Furtado M.R., Forsythe S.J.;
RT "Comparative analysis of genome sequences covering the seven cronobacter
RT species.";
RL PLoS ONE 7:e49455-e49455(2012).
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}.
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:CCJ81885.1}.
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DR EMBL; CAKZ01000117; CCJ81885.1; -; Genomic_DNA.
DR AlphaFoldDB; K8B696; -.
DR Proteomes; UP000009342; Unassembled WGS sequence.
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:CCJ81885.1}.
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; 36457 MW; D3E04AF19967D25D CRC64;
MIDLRSDTVT RPGNAMLERM MAAPTGDDVY GDDPTVNALQ EYAARLSGKE GALFLPTGTQ
ANLVALLSHC ERGEEYIVGQ LAHNYLYEAG GAAVLGSIQP QPIDANGDGT LPLDKVAAKI
KPDDVHFART RLLSLENTHN GKVLPRDYLH QAWEFTRERG LALHVDGARI FNAVVAYGCE
LKDIAQYCDT FTICLSKGLG APVGSLLLGS HDYLQRAKRW RKMTGGGMRQ AGILAAAGLY
ALEHNVARLK EDHDNAAWLA GALRDAGADV RRHDTNMLFI SVPQAQVAAL GAFMKSRDVL
ISAAPVTRLV THLDVNRAQL ETVVAYWREF LQQAA
//