ID K0NCE9_DESTT Unreviewed; 361 AA.
AC K0NCE9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=CobD: threonine-phosphate decarboxylase {ECO:0000313|EMBL:CCK82144.1};
DE EC=4.1.1.81 {ECO:0000313|EMBL:CCK82144.1};
GN Name=cobD {ECO:0000313|EMBL:CCK82144.1};
GN OrderedLocusNames=TOL2_C39890 {ECO:0000313|EMBL:CCK82144.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK82144.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK82144.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO203503; CCK82144.1; -; Genomic_DNA.
DR RefSeq; WP_014959324.1; NC_018645.1.
DR AlphaFoldDB; K0NCE9; -.
DR STRING; 651182.TOL2_C39890; -.
DR KEGG; dto:TOL2_C39890; -.
DR PATRIC; fig|651182.5.peg.4695; -.
DR HOGENOM; CLU_017584_3_2_7; -.
DR OrthoDB; 9813612at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:CCK82144.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT DOMAIN 22..341
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 361 AA; 40701 MW; 9009C5457DD2E929 CRC64;
MIIGHGGNKA NLAETLGCGV DEIVDMSSNL NPLGPPENIE KVICDNLVKI RSLPEADAVT
MRKGFAHFHG IDHENVVAGN GTTWFIYTIP KALASKKVLI AGPTYSDYKD ACLMHNIDFA
HCLAKEPKMF APDIDDLSRM AKDADTVFLC NPNNPTGALM PREQLDYLIQ KHENTVFIID
ESYLPFVDQA REISLVSETG YKNLIVLSSM SKIFRIPGLR TGFLSASRKL AEKIMACYQP
WSVNALAQTV IEHIFDHPEK IEPFYQKTRD YIKTEKQLFL ESLEDIQELK LLDSTTYFIL
ARLTNGLTSE EFCKKIGQHK ILIRDCSNFL GLSDQYVRFS LKQRSVNLHL AELIKQAVKN
D
//