KDGA_SULTO
ID KDGA_SULTO Reviewed; 290 AA.
AC F9VPG1;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
DE EC=4.1.2.55 {ECO:0000269|PubMed:17176250};
GN Name=kdgA; OrderedLocusNames=STK_24790;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=17176250; DOI=10.1042/bj20061419;
RA Wolterink-van Loo S., van Eerde A., Siemerink M.A., Akerboom J.,
RA Dijkstra B.W., van der Oost J.;
RT "Biochemical and structural exploration of the catalytic capacity of
RT Sulfolobus KDG aldolases.";
RL Biochem. J. 403:421-430(2007).
CC -!- FUNCTION: Involved in the degradation of glucose and galactose via the
CC Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-
CC 3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG)
CC forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde,
CC respectively. It is also able to catalyze the reversible cleavage of 2-
CC keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-
CC deoxygalactonate (KDGal). {ECO:0000269|PubMed:17176250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-
CC phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.55;
CC Evidence={ECO:0000269|PubMed:17176250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde
CC 3-phosphate + pyruvate; Xref=Rhea:RHEA:24464, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:58298, ChEBI:CHEBI:59776; EC=4.1.2.55;
CC Evidence={ECO:0000269|PubMed:17176250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for pyruvate (at pH 6 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17176250};
CC KM=3.9 mM for D-glyceraldehyde (at pH 6 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17176250};
CC Vmax=17.8 umol/min/mg enzyme with pyruvate as substrate (at pH 6 and
CC at 70 degrees Celsius) {ECO:0000269|PubMed:17176250};
CC Vmax=20.3 umol/min/mg enzyme with D-glyceraldehyde as substrate (at
CC pH 6 and at 70 degrees Celsius) {ECO:0000269|PubMed:17176250};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:17176250};
CC Temperature dependence:
CC Optimum temperature is around 90 degrees Celsius. Extremely
CC thermostable. {ECO:0000269|PubMed:17176250};
CC -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC 3-deoxy-D-gluconate: step 2/2.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DapA family. KDPG aldolase subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000023; BAK54808.1; -; Genomic_DNA.
DR RefSeq; WP_052846807.1; NC_003106.2.
DR AlphaFoldDB; F9VPG1; -.
DR SMR; F9VPG1; -.
DR STRING; 273063.STK_24790; -.
DR EnsemblBacteria; BAK54808; BAK54808; STK_24790.
DR GeneID; 1460562; -.
DR KEGG; sto:STK_24790; -.
DR PATRIC; fig|273063.9.peg.2800; -.
DR eggNOG; arCOG04172; Archaea.
DR OMA; VVPPVCT; -.
DR OrthoDB; 65776at2157; -.
DR BRENDA; 4.1.2.55; 15396.
DR UniPathway; UPA00856; UER00829.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0008674; F:2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity; IDA:UniProtKB.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..290
FT /note="2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-
FT deoxy-6-phosphogalactonate aldolase"
FT /id="PRO_0000422657"
FT ACT_SITE 155
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129..131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155..157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 129
FT /note="Proton shuttle"
FT /evidence="ECO:0000250"
SQ SEQUENCE 290 AA; 32598 MW; 62D9FEC7E5E79B67 CRC64;
MDIVTPILTP FTKEGKIDVE KLKAHAKFLI DNGIDLLFVN GTTGLGPALS KEEKLTTLKT
IYDVTNKVIF QVGSLNINDV IDLVKASKDF DIVGIASYPP FYFPRLPEKF LLKYFTTIAN
YSPHSLYIYN YPLATGYDIS AKIVYQMKDL ITGLKDTNQD LSHSLEYKIL MPNLKVYNGS
DSLVFYSLTS LDGSVTAASN YLPHVMKKMK EHITSGQVSK AIELQKLINK ALDISRKYGQ
LSAIYYLVKE FLGYDVGYPR GPIFPLEEDE VKALLSEIQP VKKEIERAVS
