PDXA2_BORBR
ID PDXA2_BORBR Reviewed; 351 AA.
AC A0A0H3LQK8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
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=BB3214 {ECO:0000312|EMBL:CAE33706.1};
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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=0.037 mM for D-threonate 4-phosphate
CC {ECO:0000269|PubMed:27402745};
CC KM=0.039 mM for 4-hydroxy-L-threonine 4-phosphate
CC {ECO:0000269|PubMed:27402745};
CC Note=kcat is 6.9 sec(-1) with D-threonate 4-phosphate as substrate.
CC kcat is 2.2 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; BX640446; CAE33706.1; -; Genomic_DNA.
DR RefSeq; WP_003810611.1; NC_002927.3.
DR AlphaFoldDB; A0A0H3LQK8; -.
DR SMR; A0A0H3LQK8; -.
DR STRING; 257310.BB3214; -.
DR EnsemblBacteria; CAE33706; CAE33706; BB3214.
DR GeneID; 56479324; -.
DR KEGG; bbr:BB3214; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_4; -.
DR OMA; PINKLAW; -.
DR OrthoDB; 1414545at2; -.
DR Proteomes; UP000001027; 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.
FT CHAIN 1..351
FT /note="D-threonate 4-phosphate dehydrogenase"
FT /id="PRO_0000439815"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 177
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 221
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="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 284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 351 AA; 36432 MW; 76C79073000CF1BD CRC64;
MTQDATPSRI PTLAVTLGDV AGIGPEITAK MLLGHDELRQ RARLLVVGDA AVLAQAVQAV
GGDPARVRVI ATPAEATNQP GSIEVIQAGP SLAHVPPGQL SAEAGDGSVR YVTTACALAR
DGLIDGIVTA PLNKAAMHMA GHKWPGHTEL LAHEFGVKTF SLVLSAGDLY IFHATTHVSL
RQAIEDVNPQ RMRAVLRLAG SFARALGRAD HPVAVAGLNP HAGENGIFGT EDAEILAPAV
AQANAEGILA AGPIPADALF PQAVRGKWKF VIACYHDQGH APFKSVYGDD GVNITVGLPV
VRVSVDHGTA FDIAGKGIAR EDSLVLAAER AAQLAPGWHQ VWETARSTTG G
