GADH_THEAC
ID GADH_THEAC Reviewed; 493 AA.
AC Q9HK01;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=D-glyceraldehyde dehydrogenase (NADP(+)) {ECO:0000303|PubMed:16566751};
DE Short=GADH {ECO:0000303|PubMed:16566751};
DE Short=Glyceraldehyde DH {ECO:0000303|PubMed:16566751};
DE EC=1.2.1.89 {ECO:0000269|PubMed:16458304, ECO:0000269|PubMed:16566751};
GN OrderedLocusNames=Ta0809 {ECO:0000312|EMBL:CAC11938.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=16566751; DOI=10.1042/bj20051763;
RA Jung J.H., Lee S.B.;
RT "Identification and characterization of Thermoplasma acidophilum
RT glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde
RT dehydrogenase.";
RL Biochem. J. 397:131-138(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16458304; DOI=10.1016/j.febslet.2006.01.029;
RA Reher M., Schoenheit P.;
RT "Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota
RT Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-
RT phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family
RT within the aldehyde dehydrogenase superfamily.";
RL FEBS Lett. 580:1198-1204(2006).
CC -!- FUNCTION: NADP-dependent dehydrogenase of the nED (non-phosphorylated
CC Entner-Doudoroff) pathway with highest activity towards glyceraldehydes
CC (e.g. D,L-glyceraldehyde and D-glyceraldehyde), to a lesser extent
CC towards D,L-glyceraldehyde-3-phosphate and glycolaldehyde, but no
CC activity towards aliphatic or aromatic aldehydes.
CC {ECO:0000269|PubMed:16458304, ECO:0000269|PubMed:16566751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde + H2O + NADP(+) = (R)-glycerate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:40163, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16659, ChEBI:CHEBI:17378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.89;
CC Evidence={ECO:0000269|PubMed:16458304, ECO:0000269|PubMed:16566751};
CC -!- ACTIVITY REGULATION: Inhibited by calcium, cadmium, copper and mercury
CC ions. Stable for 2 hours at 60 degrees Celsius but activity is
CC decreased to less than 50 percent within 20 minutes at 80 degrees
CC Celsius. Two folds activity enhancement in the presence of 1 mM
CC glutathione, DTT, or 2-mercaptoethanol. Complete activity inhibition by
CC thiol-modifying reagents such as p-chloromercuribenzoic acid or p-
CC hydroxy-mercuribenzoic acid. {ECO:0000269|PubMed:16566751}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for glyceraldehyde (at pH 7.9 and 58 degrees Celsius)
CC {ECO:0000269|PubMed:16458304};
CC KM=18.3 mM for glyceraldehyde-3-phosphate (at pH 7.9 and 58 degrees
CC Celsius) {ECO:0000269|PubMed:16458304};
CC KM=12.3 mM for glycolaldehyde (at pH 7.9 and 58 degrees Celsius)
CC {ECO:0000269|PubMed:16458304};
CC KM=0.36 mM for NADP (at pH 7.9 and 58 degrees Celsius)
CC {ECO:0000269|PubMed:16458304};
CC KM=0.33 mM for D,L-glyceraldehyde (at pH 8 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:16566751};
CC KM=0.017 mM for NADP (at pH 8 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:16566751};
CC Vmax=0.3 umol/min/mg enzyme with D,L-glyceraldehyde as substrate (at
CC pH 8 and 50 degrees Celsius) {ECO:0000269|PubMed:16566751};
CC Vmax=0.3 umol/min/mg enzyme with NADP as substrate (at pH 8 and 50
CC degrees Celsius) {ECO:0000269|PubMed:16566751};
CC Note=kcat is 26 sec(-1) with glyceraldehyde as substrate, 20 sec(-1)
CC with glyceraldehyde-3-phosphate as substrate, 37 sec(-1) with
CC glycolaldehyde as substrate and 25 sec(-1) with NADP as substrate (at
CC pH 7.9 and 58 degrees Celsius). {ECO:0000269|PubMed:16458304};
CC pH dependence:
CC Optimum pH is 7.6-8. {ECO:0000269|PubMed:16458304,
CC ECO:0000269|PubMed:16566751};
CC Temperature dependence:
CC Optimum temperature is 50-55 degrees Celsius at pH 8 and 63 degrees
CC Celsius at pH 7.6. {ECO:0000269|PubMed:16458304,
CC ECO:0000269|PubMed:16566751};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC {ECO:0000303|PubMed:16566751}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000269|PubMed:16458304,
CC ECO:0000269|PubMed:16566751}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC Glyceraldehyde dehydrogenase subfamily. {ECO:0000255|RuleBase:RU003345,
CC ECO:0000305}.
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DR EMBL; AL445065; CAC11938.1; -; Genomic_DNA.
DR RefSeq; WP_010901221.1; NC_002578.1.
DR PDB; 5IZD; X-ray; 2.05 A; A/B/C/D/E/F/G/H=1-493.
DR PDB; 5J77; X-ray; 2.10 A; A/B/C/D=1-493.
DR PDB; 5M4X; X-ray; 3.56 A; A/B/C/D=1-493.
DR PDBsum; 5IZD; -.
DR PDBsum; 5J77; -.
DR PDBsum; 5M4X; -.
DR AlphaFoldDB; Q9HK01; -.
DR SMR; Q9HK01; -.
DR STRING; 273075.Ta0809; -.
DR EnsemblBacteria; CAC11938; CAC11938; CAC11938.
DR GeneID; 1456354; -.
DR KEGG; tac:Ta0809; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_1_0_2; -.
DR OMA; NDDLGEV; -.
DR OrthoDB; 56373at2157; -.
DR BRENDA; 1.2.1.89; 6324.
DR SABIO-RK; Q9HK01; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0043796; F:glyceraldehyde dehydrogenase (NADP) activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009255; P:Entner-Doudoroff pathway through 6-phosphogluconate; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..493
FT /note="D-glyceraldehyde dehydrogenase (NADP(+))"
FT /id="PRO_0000430740"
FT COILED 70..92
FT /evidence="ECO:0000255"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 281
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 146..149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172..176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q59931,
FT ECO:0000250|UniProtKB:Q84DC3"
FT BINDING 204..210
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q84DC3"
FT BINDING 225..248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q59931"
FT BINDING 281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q84DC3"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 381..383
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037,
FT ECO:0000250|UniProtKB:Q59931"
FT SITE 149
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5IZD"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 39..77
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 94..112
FT /evidence="ECO:0007829|PDB:5IZD"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:5IZD"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:5IZD"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:5IZD"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:5J77"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 418..427
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:5IZD"
FT STRAND 468..476
FT /evidence="ECO:0007829|PDB:5IZD"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:5IZD"
SQ SEQUENCE 493 AA; 54782 MW; 2F6A79DD96BE7FF5 CRC64;
MDTKLYIDGQ WVNSSSGKTV DKYSPVTGQV IGRFEAATRD DVDRAIDAAE DAFWAWNDLG
SVERSKIIYR AKELIEKNRA ELENIIMEEN GKPVKEAKEE VDGVIDQIQY YAEWARKLNG
EVVEGTSSHR KIFQYKVPYG IVVALTPWNF PAGMVARKLA PALLTGNTVV LKPSSDTPGS
AEWIVRKFVE AGVPKGVLNF ITGRGSEIGD YIVEHKKVNL ITMTGSTATG QRIMQKASAN
MAKLILELGG KAPFMVWKDA DMDNALKTLL WAKYWNAGQS CIAAERLYVH EDIYDTFMSR
FVELSRKLAL GDPKNADMGP LINKGALQAT SEIVEEAKES GAKILFGGSQ PSLSGPYRNG
YFFLPTIIGN ADQKSKIFQE EIFAPVIGAR KISSVEEMYD LANDSKYGLA SYLFTKDPNI
IFEASERIRF GELYVNMPGP EASQGYHTGF RMTGQAGEGS KYGISEYLKL KNIYVDYSGK
PLHINTVRDD LFQ
