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Database: UniProt
Entry: R7RPV5_9CLOT
LinkDB: R7RPV5_9CLOT
Original site: R7RPV5_9CLOT 
ID   R7RPV5_9CLOT            Unreviewed;       344 AA.
AC   R7RPV5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:CDF57401.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:CDF57401.1};
GN   ORFNames=TCEL_01315 {ECO:0000313|EMBL:CDF57401.1};
OS   Thermobrachium celere DSM 8682.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermobrachium.
OX   NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF57401.1, ECO:0000313|Proteomes:UP000014923};
RN   [1] {ECO:0000313|EMBL:CDF57401.1, ECO:0000313|Proteomes:UP000014923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF57401.1,
RC   ECO:0000313|Proteomes:UP000014923};
RA   Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT   "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT   alkalithermophilic Caloramator celere.";
RL   Submitted (MAR-2013) 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}.
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:CDF57401.1}.
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DR   EMBL; CAVN010000087; CDF57401.1; -; Genomic_DNA.
DR   RefSeq; WP_018660511.1; NZ_HF952018.1.
DR   AlphaFoldDB; R7RPV5; -.
DR   eggNOG; COG2008; Bacteria.
DR   HOGENOM; CLU_049619_0_0_9; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000014923; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CDF57401.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014923}.
FT   DOMAIN          4..289
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
SQ   SEQUENCE   344 AA;  39585 MW;  CF33EF49A31971AA CRC64;
     MKSFASDNTS RVHPKIMESI VNANNYDAKS YGYDEYTQRA VEKFKKLFGD DIDVYFVYNG
     TAANILGLSA ITNTYNSIIC SEWAHINTDE CGAPEKNIGC KIISLSSSDG KIKVEDINKH
     LFAIGVEHHS QPKVISITQS TELGTVYTKE EIIEISEFAH KNNMYVHMDG ARIANAACHL
     KQDVREFTKD AGVDVLSFGG TKNGMMFGEA VVFFNKNLSE GFKYRRKQFM QLHSKMRYIS
     AQFEALLTDD LYLKNARHAN EMAKYLEERL KELPIVRITQ KVEANAIFAS LPREIIDKLL
     EKYYFYIWNE EKNEVRWMTS FDTKREDIDE FVDDLNKIVK NVFK
//
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