COBD_SALTI
ID COBD_SALTI Reviewed; 364 AA.
AC Q8Z8H8;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Threonine-phosphate decarboxylase;
DE EC=4.1.1.81;
DE AltName: Full=L-threonine-O-3-phosphate decarboxylase;
GN Name=cobD; OrderedLocusNames=STY0695, t2223;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL513382; CAD05121.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69826.1; -; Genomic_DNA.
DR RefSeq; NP_455220.1; NC_003198.1.
DR RefSeq; WP_001173241.1; NZ_WSUR01000015.1.
DR AlphaFoldDB; Q8Z8H8; -.
DR SMR; Q8Z8H8; -.
DR STRING; 220341.16501895; -.
DR PRIDE; Q8Z8H8; -.
DR EnsemblBacteria; AAO69826; AAO69826; t2223.
DR KEGG; stt:t2223; -.
DR KEGG; sty:STY0695; -.
DR PATRIC; fig|220341.7.peg.699; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_2_6; -.
DR OMA; RDPWSVN; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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: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; Lyase; Pyridoxal phosphate.
FT CHAIN 1..364
FT /note="Threonine-phosphate decarboxylase"
FT /id="PRO_0000163821"
FT BINDING 8..9
FT /ligand="O-phospho-L-threonine"
FT /ligand_id="ChEBI:CHEBI:58675"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT BINDING 32
FT /ligand="O-phospho-L-threonine"
FT /ligand_id="ChEBI:CHEBI:58675"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT BINDING 157
FT /ligand="O-phospho-L-threonine"
FT /ligand_id="ChEBI:CHEBI:58675"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT BINDING 323
FT /ligand="O-phospho-L-threonine"
FT /ligand_id="ChEBI:CHEBI:58675"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT BINDING 337
FT /ligand="O-phospho-L-threonine"
FT /ligand_id="ChEBI:CHEBI:58675"
FT /evidence="ECO:0000250|UniProtKB:P97084"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P97084"
SQ SEQUENCE 364 AA; 40803 MW; EE198DEA2E6CD042 CRC64;
MALFNSAHGG NIREAATVLG ISPDQLLDFS ANINPLGMPV SVKRALIDNL DCIERYPDAD
YFHLHQALAR HHQVPASWIL AGNGETESIF TVASGLKPRR AIIVTPGFAE YGRALAQIGC
EIRRWSLREA DGWQLTDAIL EALTPDLDCL FLCTPNNPTG LLPERQLLQA IADRCKSLNI
NLILDEAFID FIPHETGFIP ALKDNPHIWV LRSLTKFYAI PGLRLGYLVN SDDAAVARMR
RQQMPWSVNA LAALAGEVAL QDSAWQQATW HWLREEGARF YQALCQLPLL TVYPGRANYL
LLRCEREDID LQRRLLTQRI LIRSCANYPG LDSRYYRVAI RSAAQNERLL AALRNVLTGI
TPAD
