ID   COBC_PSEAE              Reviewed;         331 AA.
AC   Q9I468;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Threonine-phosphate decarboxylase;
DE            EC=4.1.1.81;
DE   AltName: Full=L-threonine-O-3-phosphate decarboxylase;
GN   Name=cobC; OrderedLocusNames=PA1276;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   ---------------------------------------------------------------------------
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; AE004091; AAG04665.1; -; Genomic_DNA.
DR   PIR; B83486; B83486.
DR   RefSeq; NP_249967.1; NC_002516.2.
DR   RefSeq; WP_003112352.1; NZ_QZGE01000005.1.
DR   AlphaFoldDB; Q9I468; -.
DR   SMR; Q9I468; -.
DR   STRING; 287.DR97_659; -.
DR   PaxDb; Q9I468; -.
DR   PRIDE; Q9I468; -.
DR   EnsemblBacteria; AAG04665; AAG04665; PA1276.
DR   GeneID; 881414; -.
DR   KEGG; pae:PA1276; -.
DR   PATRIC; fig|208964.12.peg.1326; -.
DR   PseudoCAP; PA1276; -.
DR   HOGENOM; CLU_017584_3_4_6; -.
DR   InParanoid; Q9I468; -.
DR   OMA; RDPWSVN; -.
DR   PhylomeDB; Q9I468; -.
DR   BioCyc; PAER208964:G1FZ6-1301-MON; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002438; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..331
FT                   /note="Threonine-phosphate decarboxylase"
FT                   /id="PRO_0000287744"
FT   MOD_RES         192
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  36657 MW;  5C4D624C54477022 CRC64;
     MLEHGGRLRE AARRYDIPLA DWLDLSTGIA PWPFSLPAIP EQAWTRLPES DDGLEAAACL
     YYGAERVLPL AGSQAAIQAL PRMRRGGRVG VLSPCYAEHA HAWRQAGHLV REIGEAEVEP
     YLDSLDVLLV VNPNNPTGRV FEPAELLAWH ARLQRRGGWL LVDEAFMDCT PQSSLAACSN
     RPGLIVLRSF GKFFGLAGAR LGFALGERPL LQALAEQLGP WTVNGPVRHV AQSALRDRQQ
     QRQQRERLLA ASQRLEELLR RHGWPPAGGS ALFQRLVDPR CAALHDYLAR RGILTRQFEQ
     PASLRLGLPA DEAAWARLDA ALLGFKEPAH E