ID M5BSZ3_THACB Unreviewed; 379 AA.
AC M5BSZ3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:CCO30341.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:CCO30341.1};
GN ORFNames=BN14_04368 {ECO:0000313|EMBL:CCO30341.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO30341.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO30341.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
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}.
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:CCO30341.1}.
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DR EMBL; CAOJ01006309; CCO30341.1; -; Genomic_DNA.
DR AlphaFoldDB; M5BSZ3; -.
DR HOGENOM; CLU_029381_1_0_1; -.
DR Proteomes; UP000012065; 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:CCO30341.1}.
FT DOMAIN 20..304
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 379 AA; 40581 MW; F6FB9BB4FECF02F5 CRC64;
MTETTLHPSI SQANALSAVD FRSDTVTSPT AAMLHAMISS AVGDDVYSED ETTANLERHV
ADLLGHEAGL FVPSGTAGNQ IAIRVHLTQP PHSVLCHARS HINQYEAGGI ATLSQAMVQP
VWPSKGPNLT LEDVKKGVVL WDDIHCAPTR VIALENTYGG TILPLNEVQL ISEFARSNNI
RIHCDGARLW NAVAAGAGSF REYGAAFDSI SLCFSKGIGA PVGSVLVGSK IFIDRARWIR
KSIGGGMRQT GVIAGAARAA LDEVFPKLAA THEIARDIEK HLHSLGLKTV LPVETNMIFI
DLQAAGLDND WLIEEANSEG LRLGYDGRIV VHHQISTEAV KKLKEILSRV MEKKAAGAYA
QASQAQVNGG TYGGMPKRT
//
