ID PDXA2_SALTY Reviewed; 327 AA. AC P58718; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=D-threonate 4-phosphate dehydrogenase {ECO:0000303|PubMed:27402745}; DE EC=1.1.1.408 {ECO:0000269|PubMed:27402745}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000303|PubMed:27294475}; DE Short=4PHT dehydrogenase {ECO:0000303|PubMed:27294475}; GN Name=pdxA2 {ECO:0000303|PubMed:27294475, ECO:0000303|PubMed:27402745}; GN OrderedLocusNames=STM0163; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] 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 [2] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=27294475; DOI=10.1021/acschembio.6b00279; RA Thiaville J.J., Flood J., Yurgel S., Prunetti L., Elbadawi-Sidhu M., RA Hutinet G., Forouhar F., Zhang X., Ganesan V., Reddy P., Fiehn O., RA Gerlt J.A., Hunt J.F., Copley S.D., de Crecy-Lagard V.; RT "Members of a novel kinase family (DUF1537) can recycle toxic intermediates RT into an essential metabolite."; RL ACS Chem. Biol. 11:2304-2311(2016). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION RP PHENOTYPE. RC STRAIN=LT2; RX PubMed=27402745; DOI=10.1073/pnas.1605546113; RA Zhang X., Carter M.S., Vetting M.W., San Francisco B., Zhao S., RA Al-Obaidi N.F., Solbiati J.O., Thiaville J.J., de Crecy-Lagard V., RA Jacobson M.P., Almo S.C., Gerlt J.A.; RT "Assignment of function to a domain of unknown function: DUF1537 is a new RT kinase family in catabolic pathways for acid sugars."; RL Proc. Natl. Acad. Sci. U.S.A. 113:E4161-E4169(2016). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT. RG Midwest center for structural genomics (MCSG); RT "The structure of a putative 4-hydroxythreonine-4-phosphate dehydrogenase RT from Salmonella typhimurium."; RL Submitted (AUG-2006) to the PDB data bank. CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation and subsequent CC decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone CC phosphate (DHAP) (PubMed:27402745). Can also use 4-hydroxy-L-threonine CC 4-phosphate as substrate (PubMed:27294475, PubMed:27402745). CC {ECO:0000269|PubMed:27294475, ECO:0000269|PubMed:27402745}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-O-phospho-D-threonate + NAD(+) = CO2 + dihydroxyacetone CC phosphate + NADH; Xref=Rhea:RHEA:52396, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:136590; EC=1.1.1.408; CC Evidence={ECO:0000269|PubMed:27402745}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P19624}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000250|UniProtKB:P19624}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.054 mM for D-threonate 4-phosphate CC {ECO:0000269|PubMed:27402745}; CC KM=0.19 mM for 4-hydroxy-L-threonine 4-phosphate CC {ECO:0000269|PubMed:27402745}; CC KM=7.24 mM for 4-hydroxy-L-threonine 4-phosphate CC {ECO:0000269|PubMed:27294475}; CC Note=kcat is 8.9 sec(-1) with D-threonate 4-phosphate as substrate. CC kcat is 0.37 sec(-1) with 4-hydroxy-L-threonine 4-phosphate as CC substrate (PubMed:27402745). kcat is 0.06 sec(-1) with CC 4-hydroxy-L-threonine 4-phosphate as substrate (PubMed:27294475). CC {ECO:0000269|PubMed:27294475, ECO:0000269|PubMed:27402745}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.4}. CC -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to use D-threonate as a CC carbon source. {ECO:0000269|PubMed:27402745}. CC -!- SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily. {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; AE006468; AAL19127.1; -; Genomic_DNA. DR RefSeq; NP_459168.1; NC_003197.2. DR RefSeq; WP_000448745.1; NC_003197.2. DR PDB; 2HI1; X-ray; 2.30 A; A/B=1-327. DR PDBsum; 2HI1; -. DR AlphaFoldDB; P58718; -. DR SMR; P58718; -. DR STRING; 99287.STM0163; -. DR PaxDb; 99287-STM0163; -. DR GeneID; 1251681; -. DR KEGG; stm:STM0163; -. DR PATRIC; fig|99287.12.peg.173; -. DR HOGENOM; CLU_040168_1_0_6; -. DR OMA; APDTVFM; -. DR PhylomeDB; P58718; -. DR BioCyc; MetaCyc:STM0163-MONOMER; -. DR BioCyc; SENT99287:STM0163-MONOMER; -. DR BRENDA; 1.1.1.408; 5542. DR BRENDA; 1.1.1.409; 5542. DR EvolutionaryTrace; P58718; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR005255; PdxA_fam. DR NCBIfam; TIGR00557; pdxA; 1. DR PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR30004:SF6; D-THREONATE 4-PHOSPHATE DEHYDROGENASE; 1. DR Pfam; PF04166; PdxA; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1..327 FT /note="D-threonate 4-phosphate dehydrogenase" FT /id="PRO_0000188828" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 169 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 213 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 268 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 276 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 285 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT BINDING 294 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P19624" FT STRAND 6..9 FT /evidence="ECO:0007829|PDB:2HI1" FT TURN 13..16 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 17..25 FT /evidence="ECO:0007829|PDB:2HI1" FT TURN 28..32 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 41..49 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 57..63 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 94..112 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 126..131 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 139..146 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 172..178 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 181..197 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 204..208 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 222..226 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 228..236 FT /evidence="ECO:0007829|PDB:2HI1" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 241..246 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 248..256 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 261..267 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 268..277 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:2HI1" FT STRAND 290..298 FT /evidence="ECO:0007829|PDB:2HI1" FT TURN 303..309 FT /evidence="ECO:0007829|PDB:2HI1" FT HELIX 314..326 FT /evidence="ECO:0007829|PDB:2HI1" SQ SEQUENCE 327 AA; 35065 MW; 03BB6725F1896440 CRC64; METKTVAITM GDPAGIGPEI IVKALSEDGL NGAPLVVIGC LATLKRLQAK GITPNVELRA IERVAEARFA PGIIHVIDEP LAQPEALEAG KVQAQAGDLA YRCVKRATEL ALRGDVQAIA TAPLNKEALH LAGHNYPGHT ELLATLTHSR DYAMVLYTDK LKVIHVSTHI ALRKFLDTLS TARVETVIGI ADTFLKRVGY VKPRIAVAGV NPHAGENGLF GDEETRILTP AITDARAKGM DVYGPCPPDT VFLQAYEGQY DMVVAMYHDQ GHIPLKLLGF YDGVNITAGL PFIRTSADHG TAFDIAWTGK AKSESMAVSI KLAMQLA //