PDXA2_PECAS
ID PDXA2_PECAS Reviewed; 326 AA.
AC Q6D0N8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=ECA3760 {ECO:0000312|EMBL:CAG76659.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=SCRI 1043 / ATCC BAA-672;
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=0.025 mM for D-threonate 4-phosphate
CC {ECO:0000269|PubMed:27402745};
CC KM=0.26 mM for 4-hydroxy-L-threonine 4-phosphate
CC {ECO:0000269|PubMed:27402745};
CC Note=kcat is 8.6 sec(-1) with D-threonate 4-phosphate as substrate.
CC kcat is 2.9 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; BX950851; CAG76659.1; -; Genomic_DNA.
DR RefSeq; WP_011095261.1; NC_004547.2.
DR AlphaFoldDB; Q6D0N8; -.
DR SMR; Q6D0N8; -.
DR STRING; 218491.ECA3760; -.
DR EnsemblBacteria; CAG76659; CAG76659; ECA3760.
DR KEGG; eca:ECA3760; -.
DR PATRIC; fig|218491.5.peg.3814; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_6; -.
DR OMA; PINKLAW; -.
DR OrthoDB; 1414545at2; -.
DR Proteomes; UP000007966; 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 Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..326
FT /note="D-threonate 4-phosphate dehydrogenase"
FT /id="PRO_0000439818"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 168
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 212
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 267
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 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 326 AA; 34952 MW; ECFB0A53945DE415 CRC64;
MSKIIAVTMG DPAGIGPEII IKSLAEGELS GASAVVVGCV QTMRRILALN VVPTVELKII
DKPADAVFAP GVINIIDEPL EDPQALKPGI VQAQAGDLAY RCIKKATALA MAGEVHAIAT
APLNKEALHS AGHLYPGHTE LLAKLTNSRD YAMVLYTDKL KVIHVSTHIA LRKFLDTLNR
DRVETVIEMA DVFLKRVGFT HPRIAVAGVN PHAGENGLFG DEEIKIVSPS VEAMKAKGID
VYGPCPPDTV YLQAYEGQYD MVVAMYHDQG HIPLKLLGFY DGVNITAGLP FIRTSADHGT
AFDIAWTGKA KPESMAISIQ LAMQLA
