PDXA2_CUPNH
ID PDXA2_CUPNH Reviewed; 333 AA.
AC Q0K4F5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=D-threonate 4-phosphate dehydrogenase {ECO:0000303|PubMed:27402745};
DE EC=1.1.1.408 {ECO:0000269|PubMed:27402745};
GN Name=pdxA2 {ECO:0000303|PubMed:27402745};
GN OrderedLocusNames=H16_B0319 {ECO:0000312|EMBL:CAJ95119.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
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).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation and subsequent
CC decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone
CC phosphate (DHAP). Can also use 4-hydroxy-L-threonine 4-phosphate as
CC substrate. {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=0.12 mM for D-threonate 4-phosphate {ECO:0000269|PubMed:27402745};
CC KM=0.20 mM for 4-hydroxy-L-threonine 4-phosphate
CC {ECO:0000269|PubMed:27402745};
CC Note=kcat is 3.4 sec(-1) with D-threonate 4-phosphate as substrate.
CC kcat is 0.35 sec(-1) with 4-hydroxy-L-threonine 4-phosphate as
CC substrate. {ECO:0000269|PubMed:27402745};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P58718}.
CC -!- SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily. {ECO:0000305}.
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DR EMBL; AM260480; CAJ95119.1; -; Genomic_DNA.
DR RefSeq; WP_011616489.1; NZ_CP039288.1.
DR AlphaFoldDB; Q0K4F5; -.
DR SMR; Q0K4F5; -.
DR STRING; 381666.H16_B0319; -.
DR EnsemblBacteria; CAJ95119; CAJ95119; H16_B0319.
DR GeneID; 57646201; -.
DR KEGG; reh:H16_B0319; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_4; -.
DR OMA; PINKLAW; -.
DR OrthoDB; 1414545at2; -.
DR BRENDA; 1.1.1.408; 231.
DR BRENDA; 1.1.1.409; 231.
DR Proteomes; UP000008210; Chromosome 2.
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 Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..333
FT /note="D-threonate 4-phosphate dehydrogenase"
FT /id="PRO_0000439816"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 170
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 214
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 270
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 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 333 AA; 35491 MW; 3139BF86A1AAF1CB CRC64;
MSDYLPVIGI TMGDATGIGP EVIVKSLAHD SVRAQCRPLV IGDVRRLEVA GRLVGSPLKL
RAIQAPEEAR FQSGTIDCID LGLIPEGLPF GKLSAVAGDA AFRYIERAVA LTRDEKIDAI
CTAPLNKEAL HAGGHKFPGH TEMLAYLTGT PEVSMMLVAP KLRVIHVTTH IGLLDAIRKI
EPGLVQRTIE RGHQTLQRAG IAAPRIGVCG INPHAGENGL FGHGEEEEKI IPAVEALRAR
GRDVEGPLPA DTLFYRAGRG DFDLVVAMYH DQGHGPVKVL GLEAGVNITV GLPVIRTSVD
HGTAFDIAGK GIADERSLLE ALRQGAELAT RRA
