ID B8E1W7_DICTD Unreviewed; 343 AA.
AC B8E1W7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:ACK41750.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:ACK41750.1};
GN OrderedLocusNames=Dtur_0449 {ECO:0000313|EMBL:ACK41750.1};
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC Dictyoglomus.
OX NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK41750.1, ECO:0000313|Proteomes:UP000007719};
RN [1] {ECO:0000313|Proteomes:UP000007719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310 {ECO:0000313|Proteomes:UP000007719};
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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}.
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DR EMBL; CP001251; ACK41750.1; -; Genomic_DNA.
DR RefSeq; WP_012582835.1; NC_011661.1.
DR RefSeq; YP_002352364.1; NC_011661.1.
DR AlphaFoldDB; B8E1W7; -.
DR STRING; 515635.Dtur_0449; -.
DR EnsemblBacteria; ACK41750; ACK41750; Dtur_0449.
DR KEGG; dtu:Dtur_0449; -.
DR PATRIC; fig|515635.4.peg.474; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_4_0; -.
DR InParanoid; B8E1W7; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000007719; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IBA:GO_Central.
DR GO; GO:0006545; P:glycine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
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 Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:ACK41750.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007719}.
FT DOMAIN 5..287
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT COILED 243..270
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 343 AA; 38559 MW; 16407AC223EBCA8F CRC64;
MRFIDLRSDT VTKPTEEMRK AMYEAEVGDD GYGEDPTVNL LEQKAAELLG KEAGLFVVSG
TMGNQVALLT WTRPGDEVIL ESESHIYYYE AGGMAGNSGV QPFLIDGEEG VMPIEEIEKA
IRPKGRVFPK TSLIVLENTH NRAGGKVLPL EYMKEVYEIS RKHDIPIHLD GARIFNAAIY
LGIPAKEIAK YADSVMFCLS KGLSCPMGSV LVGSKEFIEE ARRKRQRLGG GLRQAGVVAA
CGIVALERMI DRLVEDHEKA QNLYNFLKDI EIFSVKKPDT NILKVRIKIN KKAREFLEEF
KKYGLLATSF DDETLRFVTH KDVSFEDIEK AKEIIYKVWE SIS
//
