ID I0V2X6_9PSEU Unreviewed; 376 AA.
AC I0V2X6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:EID54479.1};
GN ORFNames=SacxiDRAFT_2249 {ECO:0000313|EMBL:EID54479.1};
OS Saccharomonospora xinjiangensis XJ-54.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882086 {ECO:0000313|EMBL:EID54479.1, ECO:0000313|Proteomes:UP000004691};
RN [1] {ECO:0000313|EMBL:EID54479.1, ECO:0000313|Proteomes:UP000004691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XJ-54 {ECO:0000313|EMBL:EID54479.1,
RC ECO:0000313|Proteomes:UP000004691};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "Improved High-Quality Draft sequence of Saccharomonospora xinjiangensis
RT XJ-54.";
RL Submitted (JAN-2012) 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; JH636049; EID54479.1; -; Genomic_DNA.
DR AlphaFoldDB; I0V2X6; -.
DR STRING; 882086.SacxiDRAFT_2249; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_2_11; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000004691; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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;
FT DOMAIN 40..320
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 376 AA; 39098 MW; 714EDEB9E4FA9DE7 CRC64;
MRRAVSRING VHGELSQPCD VIGPVTVEFS GSETSTSPLD FRSDTLTVPD ERMRTAMAEA
EVGDNVIDTD PTIRRLEERV AEILGMQAAL WTPSGTMANL VALSTHLRRG DRFLAPRGAH
VLVNELGSAA WLAGGMPEAL DHDGGPGRPS PAAVRAAAGG SGPYYTLRTT LLSLENTHNS
AGGAVTPPDE HALLVAAARD AGLRVHLDGA RIWNASVALG VPPAELTAGV DSVSACFSKG
LGAPAGSVVA GSAEFVEQAR RMRQMLGGGM RQIGVLASAC LVALGRVGDL ADDHAKAAEL
AAGLRERGWE VTEPQTNIVL AGAPGGAGLA ATCDRLLALG IHVLPMAGKV RFVLHRDVRQ
GDIAEALRRI DRGLGR
//
