ID   COBC_SINSX              Reviewed;         333 AA.
AC   P21633;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Threonine-phosphate decarboxylase;
DE            EC=4.1.1.81;
DE   AltName: Full=L-threonine-O-3-phosphate decarboxylase;
GN   Name=cobC;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=2211520; DOI=10.1128/jb.172.10.5968-5979.1990;
RA   Crouzet J., Cauchois L., Blanche F., Debussche L., Thibaut D.,
RA   Rouyez M.-C., Rigault S., Mayaux J.-F., Cameron B.;
RT   "Nucleotide sequence of a Pseudomonas denitrificans 5.4-kilobase DNA
RT   fragment containing five cob genes and identification of structural genes
RT   encoding S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase
RT   and cobyrinic acid a,c-diamide synthase.";
RL   J. Bacteriol. 172:5968-5979(1990).
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:0000305};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M59236; AAA25775.1; -; Genomic_DNA.
DR   AlphaFoldDB; P21633; -.
DR   SMR; P21633; -.
DR   PRIDE; P21633; -.
DR   BioCyc; MetaCyc:MON-141; -.
DR   UniPathway; UPA00148; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Cytoplasm; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..333
FT                   /note="Threonine-phosphate decarboxylase"
FT                   /id="PRO_0000123921"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  35014 MW;  DFCA4361B69B6DDB CRC64;
     MSAPIVHGGG ITEAAARYGG RPEDWLDLST GINPCPVALP AVPERAWHRL PDRQTVDDAR
     SAAADYYRTN GVLPLPVPGT QSVIQLLPRL APANRHVAIF GPTYGEYARV LEAAGFAVDR
     VADADALTAE HGLVIVVNPN NPTGRALAPA ELLAIAARQK ASGGLLLVDE AFGDLEPQLS
     VAGHASGQGN LIVFRSFGKF FGLAGLRLGF VVATEPVLAS FADWLGPWAV SGPALTISKA
     LMQGDTKAIA AGILERRAGL DAALDGAGLN RIGGTGLFVL VEHPRAALLQ ERLCEAHILT
     RKFDYAPTWL RVGLAPDAAG DRRLADALAR MEL