ID   COBD_CALS4              Reviewed;         367 AA.
AC   Q8R5U4;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Putative threonine-phosphate decarboxylase;
DE            EC=4.1.1.81;
DE   AltName: Full=L-threonine-O-3-phosphate decarboxylase;
GN   Name=cobD; OrderedLocusNames=TTE0380;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-
CC       amino-2-propanol O-2-phosphate, the precursor for the linkage between
CC       the nucleotide loop and the corrin ring in cobalamin. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + O-phospho-L-threonine = (R)-1-aminopropan-2-yl
CC         phosphate + CO2; Xref=Rhea:RHEA:11492, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58563, ChEBI:CHEBI:58675; EC=4.1.1.81;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE008691; AAM23667.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8R5U4; -.
DR   SMR; Q8R5U4; -.
DR   STRING; 273068.TTE0380; -.
DR   EnsemblBacteria; AAM23667; AAM23667; TTE0380.
DR   KEGG; tte:TTE0380; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_2_9; -.
DR   OMA; RDPWSVN; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000555; 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:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005860; CobD.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01140; L_thr_O3P_dcar; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..367
FT                   /note="Putative threonine-phosphate decarboxylase"
FT                   /id="PRO_0000163823"
FT   BINDING         12..13
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         29
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         152
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         320
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   BINDING         334
FT                   /ligand="O-phospho-L-threonine"
FT                   /ligand_id="ChEBI:CHEBI:58675"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97084"
SQ   SEQUENCE   367 AA;  42396 MW;  292512F7EE1F8435 CRC64;
     MKEGEKMKPY EHGGNIYDYQ GNLIDFSSNI NPLGPPEWIW EAIKEVDLSR YPDIKYRRLK
     EAIAEYVGCD RENIIVGNGA AELIHLFARA FKLKKPLIPS PSFLEYERAV KLNGGEPVYL
     KLEEEEGFRV NFAKVISKIE EADGLILGNP NNPTGQGIIR EEIGILLKKA ELMNIPVLID
     EAFIEFMKDY KKYEALPLVK KHDKLFVVRA VTKFFGMPGI RLGYGIGSPS LIQKLEEYKE
     PWTVNAFAEA VGRWLFKDRE YIEKTREYVN AEIEHMLFSL RTIDYLVAFD TKVNFILLKL
     KAGTVDEVKE KLLKKGILIR DASNFRYLDK RFFRVAVKRR EDNMCLIEAL RGLYEEGVMP
     DKERVVV