ID COBD_SALTY Reviewed; 364 AA. AC P97084; Q8ZQZ9; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2003, sequence version 2. DT 10-JUN-2026, entry version 143. DE RecName: Full=Threonine-phosphate decarboxylase; DE EC=4.1.1.81 {ECO:0000269|PubMed:9446573}; DE AltName: Full=L-threonine-O-3-phosphate decarboxylase; GN Name=cobD; OrderedLocusNames=STM0644; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=LT2; RX PubMed=9446573; DOI=10.1074/jbc.273.5.2684; RA Brushaber K.R., O'Toole G.A., Escalante-Semerena J.C.; RT "CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase RT activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2- RT phosphate, a proposed new intermediate in cobalamin biosynthesis in RT Salmonella typhimurium LT2."; RL J. Biol. Chem. 273:2684-2691(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] {ECO:0007744|PDB:1LKC} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH PHOSPHATE AND RP PYRIDOXAL PHOSPHATE, COFACTOR, AND SUBUNIT. RX PubMed=11939774; DOI=10.1021/bi012111w; RA Cheong C.-G., Bauer C.B., Brushaber K.R., Escalante-Semerena J.C., RA Rayment I.; RT "Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase RT (CobD) enzyme from Salmonella enterica."; RL Biochemistry 41:4798-4808(2002). RN [4] {ECO:0007744|PDB:1LC5, ECO:0007744|PDB:1LC7, ECO:0007744|PDB:1LC8} RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEXES WITH PHOSPHOTHREONINE RP AND REACTION INTERMEDIATE, SUBUNIT, AND MASS SPECTROMETRY. RX PubMed=12119022; DOI=10.1021/bi020294w; RA Cheong C.-G., Escalante-Semerena J.C., Rayment I.; RT "Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) RT enzyme from Salmonella enterica: the apo, substrate, and product-aldimine RT complexes."; RL Biochemistry 41:9079-9089(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. CC {ECO:0000269|PubMed:9446573}. CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-threonine + H(+) = (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 Evidence={ECO:0000269|PubMed:9446573}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:11939774}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11939774, CC ECO:0000269|PubMed:12119022}. CC -!- MASS SPECTROMETRY: Mass=40666; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:12119022}; CC -!- MASS SPECTROMETRY: Mass=40894; Method=Electrospray; Note=With pyridoxal CC phosphate.; Evidence={ECO:0000269|PubMed:12119022}; CC -!- SIMILARITY: Belongs to the class-II 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; U90625; AAC79515.1; -; Genomic_DNA. DR EMBL; AE006468; AAL19595.1; -; Genomic_DNA. DR RefSeq; NP_459636.1; NC_003197.2. DR RefSeq; WP_001173255.1; NC_003197.2. DR PDB; 1LC5; X-ray; 1.46 A; A=1-364. DR PDB; 1LC7; X-ray; 1.80 A; A=1-364. DR PDB; 1LC8; X-ray; 1.80 A; A=1-364. DR PDB; 1LKC; X-ray; 1.80 A; A=1-364. DR AlphaFoldDB; P97084; -. DR SMR; P97084; -. DR STRING; 99287.STM0644; -. DR DrugBank; DB02482; Phosphonothreonine. DR DrugBank; DB03433; {3-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Amino]-2-Methyl-Propyl}-Phosphonic Acid. DR PaxDb; 99287-STM0644; -. DR GeneID; 1252164; -. DR KEGG; stm:STM0644; -. DR PATRIC; fig|99287.12.peg.680; -. DR HOGENOM; CLU_017584_3_2_6; -. DR OMA; PHVWVLR; -. DR PhylomeDB; P97084; -. DR BioCyc; MetaCyc:MONOMER-12856; -. DR BioCyc; SENT99287:STM0644-MONOMER; -. DR BRENDA; 4.1.1.81; 5542. DR UniPathway; UPA00148; -. DR EvolutionaryTrace; P97084; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB. DR GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IDA:UniProtKB. DR GO; GO:0009236; P:cobalamin biosynthetic process; IDA:UniProtKB. 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_large. 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 NCBIfam; TIGR01140; L_thr_O3P_dcar; 1. 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. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. DR PDBsum; 1LC5; -. DR PDBsum; 1LC7; -. DR PDBsum; 1LC8; -. DR PDBsum; 1LKC; -. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin biosynthesis; Lyase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1..364 FT /note="Threonine-phosphate decarboxylase" FT /id="PRO_0000163822" FT BINDING 8..9 FT /ligand="O-phospho-L-threonine" FT /ligand_id="ChEBI:CHEBI:58675" FT /evidence="ECO:0000269|PubMed:12119022, FT ECO:0007744|PDB:1LC7" FT BINDING 32 FT /ligand="O-phospho-L-threonine" FT /ligand_id="ChEBI:CHEBI:58675" FT /evidence="ECO:0000269|PubMed:12119022, FT ECO:0007744|PDB:1LC7" FT BINDING 157 FT /ligand="O-phospho-L-threonine" FT /ligand_id="ChEBI:CHEBI:58675" FT /evidence="ECO:0000269|PubMed:12119022, FT ECO:0007744|PDB:1LC7" FT BINDING 323 FT /ligand="O-phospho-L-threonine" FT /ligand_id="ChEBI:CHEBI:58675" FT /evidence="ECO:0000269|PubMed:12119022, FT ECO:0007744|PDB:1LC7" FT BINDING 337 FT /ligand="O-phospho-L-threonine" FT /ligand_id="ChEBI:CHEBI:58675" FT /evidence="ECO:0000269|PubMed:12119022, FT ECO:0007744|PDB:1LC7" FT MOD_RES 216 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000269|PubMed:11939774, FT ECO:0007744|PDB:1LKC" FT CONFLICT 6 FT /note="S -> T (in Ref. 1; AAC79515)" FT /evidence="ECO:0000305" FT CONFLICT 15 FT /note="A -> P (in Ref. 1; AAC79515)" FT /evidence="ECO:0000305" FT CONFLICT 25 FT /note="Q -> H (in Ref. 1; AAC79515)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="S -> T (in Ref. 1; AAC79515)" FT /evidence="ECO:0000305" FT CONFLICT 42..45 FT /note="VKRA -> LKPP (in Ref. 1; AAC79515)" FT /evidence="ECO:0000305" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 13..19 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 40..48 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 62..72 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 85..96 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 99..106 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 110..117 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 139..142 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:1LC5" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 161..164 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 165..178 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:1LC5" FT TURN 215..219 FT /evidence="ECO:0007829|PDB:1LC5" FT TURN 221..223 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 226..229 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 233..242 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 250..258 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 263..285 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 296..305 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:1LC7" FT HELIX 311..316 FT /evidence="ECO:0007829|PDB:1LC5" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:1LC5" FT STRAND 335..339 FT /evidence="ECO:0007829|PDB:1LC5" FT HELIX 343..356 FT /evidence="ECO:0007829|PDB:1LC5" SQ SEQUENCE 364 AA; 40766 MW; B6613FD0AB6D846C CRC64; MALFNSAHGG NIREAATVLG ISPDQLLDFS ANINPLGMPV SVKRALIDNL DCIERYPDAD YFHLHQALAR HHQVPASWIL AGNGETESIF TVASGLKPRR AMIVTPGFAE YGRALAQSGC EIRRWSLREA DGWQLTDAIL EALTPDLDCL FLCTPNNPTG LLPERPLLQA IADRCKSLNI NLILDEAFID FIPHETGFIP ALKDNPHIWV LRSLTKFYAI PGLRLGYLVN SDDAAMARMR RQQMPWSVNA LAALAGEVAL QDSAWQQATW HWLREEGARF YQALCQLPLL TVYPGRANYL LLRCEREDID LQRRLLTQRI LIRSCANYPG LDSRYYRVAI RSAAQNERLL AALRNVLTGI APAD //