GAD_PICTO
ID GAD_PICTO Reviewed; 391 AA.
AC Q6L1T2;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=D-gluconate/D-galactonate dehydratase {ECO:0000303|PubMed:20023024};
DE Short=GAD {ECO:0000303|PubMed:20023024};
DE Short=GNAD {ECO:0000303|PubMed:20023024};
DE EC=4.2.1.140 {ECO:0000269|PubMed:20023024};
DE EC=4.2.1.39 {ECO:0000269|PubMed:20023024};
DE EC=4.2.1.6 {ECO:0000269|PubMed:20023024};
GN Name=gad {ECO:0000303|PubMed:20023024}; OrderedLocusNames=PTO0485;
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, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP INDUCTION, AND SUBUNIT.
RX PubMed=20023024; DOI=10.1128/jb.01281-09;
RA Reher M., Fuhrer T., Bott M., Schonheit P.;
RT "The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic
RT euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate-
RT specific aldolase.";
RL J. Bacteriol. 192:964-974(2010).
CC -!- FUNCTION: Involved in the degradation of glucose and galactose via the
CC nonphosphorylative variant of Entner-Doudoroff pathway. Catalyzes the
CC dehydration of gluconate to produce 2-keto-3-deoxygluconate (KDG). It
CC is also able to catalyze the dehydration of galactonate to produce 2-
CC keto-3-deoxygalactonate (KDGal). {ECO:0000269|PubMed:20023024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC Xref=Rhea:RHEA:21612, ChEBI:CHEBI:15377, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:57990; EC=4.2.1.140;
CC Evidence={ECO:0000269|PubMed:20023024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC Xref=Rhea:RHEA:21612, ChEBI:CHEBI:15377, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:57990; EC=4.2.1.39;
CC Evidence={ECO:0000269|PubMed:20023024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O;
CC Xref=Rhea:RHEA:18649, ChEBI:CHEBI:12931, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57989; EC=4.2.1.140;
CC Evidence={ECO:0000269|PubMed:20023024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O;
CC Xref=Rhea:RHEA:18649, ChEBI:CHEBI:12931, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57989; EC=4.2.1.6;
CC Evidence={ECO:0000269|PubMed:20023024};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20023024};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:20023024};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mM for galactonate (at 60 degrees Celsius and pH 6.2)
CC {ECO:0000269|PubMed:20023024};
CC KM=2.5 mM for gluconate (at 60 degrees Celsius and pH 6.2)
CC {ECO:0000269|PubMed:20023024};
CC Vmax=15 umol/min/mg enzyme with gluconate as substrate (at 60 degrees
CC Celsius and pH 6.2) {ECO:0000269|PubMed:20023024};
CC Vmax=1 umol/min/mg enzyme with galactonate as substrate (at 60
CC degrees Celsius and pH 6.2) {ECO:0000269|PubMed:20023024};
CC pH dependence:
CC Optimum pH is between 6. {ECO:0000269|PubMed:20023024};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius).
CC {ECO:0000269|PubMed:20023024};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:20023024}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:20023024}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. GaD subfamily. {ECO:0000305}.
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DR EMBL; AE017261; AAT43070.1; -; Genomic_DNA.
DR RefSeq; WP_011177286.1; NC_005877.1.
DR AlphaFoldDB; Q6L1T2; -.
DR SMR; Q6L1T2; -.
DR STRING; 263820.PTO0485; -.
DR EnsemblBacteria; AAT43070; AAT43070; PTO0485.
DR GeneID; 2844873; -.
DR KEGG; pto:PTO0485; -.
DR PATRIC; fig|263820.9.peg.511; -.
DR eggNOG; arCOG01168; Archaea.
DR HOGENOM; CLU_030273_3_2_2; -.
DR OMA; PRWCFLK; -.
DR OrthoDB; 17973at2157; -.
DR BRENDA; 4.2.1.140; 7518.
DR BRENDA; 4.2.1.39; 7518.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0008869; F:galactonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0047929; F:gluconate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR PANTHER; PTHR48080; PTHR48080; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..391
FT /note="D-gluconate/D-galactonate dehydratase"
FT /id="PRO_0000422651"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 273
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000250"
FT SITE 325
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 44345 MW; 59C9211D53DCD5CD CRC64;
METIKSVDIY ELGSPGEKSS PWSSTILIVK LTSSNGNIGY GEAPTTFMTL PVKESMREVE
RVFKDQNYFN IEKNMREFYK HSFYLSRSME ATSALSAFEI ASWDLIGKDL GTPVYNLLGG
EYNSELRAYA NGWYSDCLEP DDFVSRAKEY IKKGYTAFKF DPFRNNFDRI GNDGIKKAVD
IVSAMRSELG ENIDLLIECH GRFSTKYAIK VGQALDEFNP LFIEEPIHPE MELGLFDFKR
YVNTPVALGE RLLNKEDFAR YISQGMVDIV QADLTNSKGI LEAKKISAIV ESFGGLMAFH
NAFGPVQTAA TLNVDYTLTN FLIQESFEDS WPDWKRNLFS GYRIENGHFK LSGKPGLGIT
ADEKLMEKLI YDGMEEFNKN EPSWVVSGTY K
