ID D4M756_9BACT Unreviewed; 345 AA.
AC D4M756;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:CBL27701.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:CBL27701.1};
GN ORFNames=SY1_01480 {ECO:0000313|EMBL:CBL27701.1};
OS Fretibacterium fastidiosum.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=651822 {ECO:0000313|EMBL:CBL27701.1, ECO:0000313|Proteomes:UP000008957};
RN [1] {ECO:0000313|EMBL:CBL27701.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL27701.1,
RC ECO:0000313|Proteomes:UP000008957};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Wade W., Vartoukian S.;
RT "The genome sequence of Synergistetes sp. SGP1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL27701.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL27701.1,
RC ECO:0000313|Proteomes:UP000008957};
RA Pajon A.;
RL Submitted (MAR-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; FP929056; CBL27701.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M756; -.
DR KEGG; sbr:SY1_01480; -.
DR PATRIC; fig|651822.3.peg.665; -.
DR HOGENOM; CLU_029381_0_4_0; -.
DR BioCyc; FFAS651822:G13GF-83-MONOMER; -.
DR Proteomes; UP000008957; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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; 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:CBL27701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008957}.
FT DOMAIN 3..289
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 345 AA; 37770 MW; CF1E1F04FB194FA5 CRC64;
MIDLRSDTLT LPDEPMLRTI LTARLGDDGR LDAEGRGEDL AVNELEDMAA EVSGKEAGLL
CASGTMGNQA ALLTWCRPGD TVLIDELQHL DRSEKTAFTP RFGQLKKVTY RSDASLMPNT
ASMEEELKNG PVKLICIENT HNYTGGACID LKRMAEIRSL ADRYGVPVHM DGARVFNAAA
FLGTTVKEIA RYVDSLMFCV SKGLGAPVGS LLCGTRKFIS EAKEMRKLLG GAMRQAGIIA
APAIYALKHN VERLREDNEN AQFCASLLKD LKKVKAQQNV QTNIMMLDME GAGITPQEFC
ARAKERGLLI RPIIGSFVRL VFYKGITRSD AERAAAIVRE IDGEL
//
