PDXA2_HELMI
ID PDXA2_HELMI Reviewed; 333 AA.
AC B0TBI8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=D-erythronate 4-phosphate dehydrogenase {ECO:0000303|PubMed:27402745};
DE EC=1.1.1.409 {ECO:0000269|PubMed:27402745};
GN Name=pdxA2 {ECO:0000303|PubMed:27402745};
GN ORFNames=HM1_2672 {ECO:0000312|EMBL:ABZ85201.1};
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1;
RX PubMed=18441057; DOI=10.1128/jb.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 51547 / Ice1;
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-erythronate 4-phosphate to produce
CC dihydroxyacetone phosphate (DHAP). Can also use D-threonate 4-phosphate
CC as substrate. {ECO:0000269|PubMed:27402745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-phospho-D-erythronate + NAD(+) = CO2 + dihydroxyacetone
CC phosphate + NADH; Xref=Rhea:RHEA:52408, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58766; EC=1.1.1.409;
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=0.0052 mM for D-erythronate 4-phosphate
CC {ECO:0000269|PubMed:27402745};
CC KM=0.019 mM for D-threonate 4-phosphate
CC {ECO:0000269|PubMed:27402745};
CC Note=kcat is 2.1 sec(-1) with D-erythronate 4-phosphate as substrate.
CC kcat is 0.024 sec(-1) with D-threonate 4-phosphate as substrate.
CC {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; CP000930; ABZ85201.1; -; Genomic_DNA.
DR RefSeq; WP_012283686.1; NC_010337.2.
DR AlphaFoldDB; B0TBI8; -.
DR SMR; B0TBI8; -.
DR STRING; 498761.HM1_2672; -.
DR EnsemblBacteria; ABZ85201; ABZ85201; HM1_2672.
DR KEGG; hmo:HM1_2672; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_1_9; -.
DR OMA; TAQVVMM; -.
DR OrthoDB; 1414545at2; -.
DR BioCyc; MetaCyc:MON-20187; -.
DR Proteomes; UP000008550; 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..333
FT /note="D-erythronate 4-phosphate dehydrogenase"
FT /id="PRO_0000439817"
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 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 333 AA; 35713 MW; 1E088079CD7466BE CRC64;
MQRPIIAIPM GDPAGVGPEI VVKALANEEM YRIARPLVIG DAGVLRQAMA FCGLELAVHT
VTEPAMGKFE PGVIDLIDLA NVELKQLKMG AVQAMAGNAA YECIEKSVSL AMAGQVDAIA
TTPINKEALK AAGIPHIGHT EILGHLSGAN DPLTMFQVFE LRVFFLSRHV SLRKACDMVT
TERALDYLVR CTEALRRLGV DSPKFAVAGL NPHSGEHGLF GDEEDEQIAP AIAAARERGI
NVVGPVPADS VFYFGLKGAY DAILSLYHDQ GHIATKMVDF ERTVAVTNGL PFLRTSVDHG
TAFDIAGSGK ASSVSMEEAI KLAVRYAPSF RRY
