PDXA2_SALTY
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 03-AUG-2022, entry version 121.
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; Proteobacteria; 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 4-hydroxy-L-
CC 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}.
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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; P58718; -.
DR EnsemblBacteria; AAL19127; AAL19127; STM0163.
DR GeneID; 1251681; -.
DR KEGG; stm:STM0163; -.
DR PATRIC; fig|99287.12.peg.173; -.
DR HOGENOM; CLU_040168_1_0_6; -.
DR OMA; PINKLAW; -.
DR PhylomeDB; P58718; -.
DR BioCyc; MetaCyc:STM0163-MON; -.
DR BioCyc; SENT99287:STM0163-MON; -.
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 InterPro; IPR005255; PdxA_fam.
DR PANTHER; PTHR30004; PTHR30004; 1.
DR Pfam; PF04166; PdxA; 1.
DR TIGRFAMs; TIGR00557; pdxA; 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
