GADH_PICTO
ID GADH_PICTO Reviewed; 493 AA.
AC Q6L285;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=D-glyceraldehyde dehydrogenase (NADP(+)) {ECO:0000303|PubMed:16458304};
DE Short=GADH {ECO:0000303|PubMed:16458304};
DE Short=Glyceraldehyde DH {ECO:0000303|PubMed:16458304};
DE EC=1.2.1.89 {ECO:0000269|PubMed:16458304};
GN OrderedLocusNames=PTO0332 {ECO:0000312|EMBL:AAT42917.1};
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
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}.
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};
CC -!- ACTIVITY REGULATION: Stable for 2 hours at 60 degrees Celsius but
CC activity is decreased to less than 50 percent within 15 minutes at 70
CC degrees Celsius. {ECO:0000269|PubMed:16458304}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for glyceraldehyde (at pH 6.9 and 58 degrees Celsius)
CC {ECO:0000269|PubMed:16458304};
CC KM=5.1 mM for glyceraldehyde-3-phosphate (at pH 6.9 and 58 degrees
CC Celsius) {ECO:0000269|PubMed:16458304};
CC KM=11.1 mM for glycolaldehyde (at pH 6.9 and 58 degrees Celsius)
CC {ECO:0000269|PubMed:16458304};
CC KM=0.42 mM for NADP (at pH 6.9 and 58 degrees Celsius)
CC {ECO:0000269|PubMed:16458304};
CC Note=kcat is 10 sec(-1) with glyceraldehyde as substrate, 12 sec(-1)
CC with glyceraldehyde-3-phosphate as substrate, 20 sec(-1) with
CC glycolaldehyde as substrate and 10 sec(-1) with NADP as substrate (at
CC pH 6.9 and 58 degrees Celsius). {ECO:0000269|PubMed:16458304};
CC pH dependence:
CC Optimum pH is 6.6. {ECO:0000269|PubMed:16458304};
CC Temperature dependence:
CC Optimum temperature is 63 degrees Celsius.
CC {ECO:0000269|PubMed:16458304};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC {ECO:0000303|PubMed:16458304}.
CC -!- SUBUNIT: Homotetramer (By similarity). Dimer of dimers.
CC {ECO:0000250|UniProtKB:Q9HK01, ECO:0000269|PubMed:16458304}.
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; AE017261; AAT42917.1; -; Genomic_DNA.
DR RefSeq; WP_011177133.1; NC_005877.1.
DR AlphaFoldDB; Q6L285; -.
DR SMR; Q6L285; -.
DR STRING; 263820.PTO0332; -.
DR PRIDE; Q6L285; -.
DR EnsemblBacteria; AAT42917; AAT42917; PTO0332.
DR GeneID; 2844486; -.
DR KEGG; pto:PTO0332; -.
DR PATRIC; fig|263820.9.peg.354; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_5_1_2; -.
DR OMA; NDDLGEV; -.
DR OrthoDB; 56373at2157; -.
DR BRENDA; 1.2.1.89; 7518.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000000438; 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; ISS: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; 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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..493
FT /note="D-glyceraldehyde dehydrogenase (NADP(+))"
FT /id="PRO_0000430741"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 144..147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170..174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q59931,
FT ECO:0000250|UniProtKB:Q84DC3"
FT BINDING 202..208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q84DC3"
FT BINDING 223..246
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q59931"
FT BINDING 279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q84DC3"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379..381
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037,
FT ECO:0000250|UniProtKB:Q59931"
FT SITE 147
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 493 AA; 55163 MW; 1091E23B9235EA68 CRC64;
MKIYIDGEWR DSSSGETIKK YNPSTGEVLD TFPAATRNDV DAAIDSAEDA FKRWSDMTSM
ERSKILYKAL ELISKDKDQL TDLLIKENGK VKREAMDETE GVIDQLQYYT EFERKLTGDI
VEGTSNKRKI FQYKVPYGIV IAITPWNFPA AMVIRKLAPA LLTGNTVILK PSSDTPLTAE
WLVKKFVDAG IPKGVLNLIT GKGSEIGDYI VEHKKVSLIT MTGSTSTGQR IMEKASKNMA
KLILELGGKA PFMVWKDANI ERALKSLVWA KYLNVGQSCI AAERLYIHED IYDEFMKKFI
EVSKRIKLGD PESSDMGPLI NKSAVETTEK YVDIARSSGY KILLGGKKPE LSGKYKNGYF
YEPTIIENVP QDSPLFQEEI FGPVIGAESV SSVDELYEKA NDSKYGLASY LFTEDPELIF
EASEKIRFGE LYVNMPGPEA SQGYHTGFRL TGQAGEGSKY GISEYLKLKN VYVDYSRGNL
SISTVNDDLF KNL
