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Database: UniProt
Entry: K0NCE9_DESTT
LinkDB: K0NCE9_DESTT
Original site: K0NCE9_DESTT 
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).
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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
//
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