ID E8N3K1_ANATU Unreviewed; 347 AA.
AC E8N3K1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:BAJ63015.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:BAJ63015.1};
GN OrderedLocusNames=ANT_09810 {ECO:0000313|EMBL:BAJ63015.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63015.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ63015.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-2010) 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}.
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DR EMBL; AP012029; BAJ63015.1; -; Genomic_DNA.
DR RefSeq; WP_013559406.1; NC_014960.1.
DR AlphaFoldDB; E8N3K1; -.
DR SMR; E8N3K1; -.
DR STRING; 926569.ANT_09810; -.
DR GeneID; 78349424; -.
DR KEGG; atm:ANT_09810; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_1_0; -.
DR InParanoid; E8N3K1; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000008922; 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:BAJ63015.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008922}.
FT DOMAIN 7..291
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 347 AA; 38064 MW; 9C26B7813B873523 CRC64;
MINHFIDLRS DTVTHPTPEM RQAMAQAEVG DDVMGEDPTV NRLEELAAEK MGKEAGLFVP
SGTMGNLTAI LTHCGRGDEM IVGHLSHTYL FEAGGSAALG GVHPFVLQNQ PDGTLRLEDL
RHAVREDDPH YPTTRLIILE NTHNRCGGVV LTPEYMRAVG TFAREKGLKL HVDGARIFNA
AVALGVLAVD LVRDADSVTF CLSKGLCAPV GSVLCGSREF IARARRIRKQ LGGGMRQAGI
LAAAGIVALE KMVERLAEDH RRARRLAEGL SSVKGLVVEN PQPATNMVYV RLGDMVQQDA
PQVAEELEKL GIKSHWVDSR RFRLVTHYWV NDEDISRTIH AFAQVLR
//
