KDGA_SULAC
ID KDGA_SULAC Reviewed; 288 AA.
AC Q4JC35;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 OrderedLocusNames=Saci_0225;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
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=1.1 mM for pyruvate (at pH 6 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17176250};
CC KM=6.3 mM for D-glyceraldehyde (at pH 6 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17176250};
CC Vmax=26.3 umol/min/mg enzyme with pyruvate as substrate (at pH 6 and
CC at 70 degrees Celsius) {ECO:0000269|PubMed:17176250};
CC Vmax=33.1 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 6.5. {ECO:0000269|PubMed:17176250};
CC Temperature dependence:
CC Optimum temperature is around 99 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:0000269|PubMed:17176250}.
CC -!- SIMILARITY: Belongs to the DapA family. KDPG aldolase subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000077; AAY79644.1; -; Genomic_DNA.
DR RefSeq; WP_011277145.1; NC_007181.1.
DR PDB; 2NUW; X-ray; 1.80 A; A/B=1-288.
DR PDB; 2NUX; X-ray; 2.50 A; A/B=1-288.
DR PDB; 2NUY; X-ray; 2.50 A; A/B=1-288.
DR PDBsum; 2NUW; -.
DR PDBsum; 2NUX; -.
DR PDBsum; 2NUY; -.
DR AlphaFoldDB; Q4JC35; -.
DR SMR; Q4JC35; -.
DR STRING; 330779.Saci_0225; -.
DR EnsemblBacteria; AAY79644; AAY79644; Saci_0225.
DR GeneID; 3474365; -.
DR KEGG; sai:Saci_0225; -.
DR PATRIC; fig|330779.12.peg.220; -.
DR eggNOG; arCOG04172; Archaea.
DR HOGENOM; CLU_049343_5_1_2; -.
DR OMA; VVPPVCT; -.
DR BRENDA; 4.1.2.55; 6160.
DR UniPathway; UPA00856; UER00829.
DR EvolutionaryTrace; Q4JC35; -.
DR Proteomes; UP000001018; 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 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 3D-structure; Carbohydrate metabolism; Lyase; Reference proteome;
KW Schiff base.
FT CHAIN 1..288
FT /note="2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-
FT deoxy-6-phosphogalactonate aldolase"
FT /id="PRO_0000422656"
FT ACT_SITE 153
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000269|PubMed:17176250"
FT BINDING 42..43
FT /ligand="substrate"
FT BINDING 129..131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153..155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 129
FT /note="Proton shuttle"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2NUW"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2NUW"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2NUW"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2NUW"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:2NUW"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:2NUW"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2NUW"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2NUW"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:2NUW"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:2NUW"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 216..234
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:2NUW"
FT HELIX 266..286
FT /evidence="ECO:0007829|PDB:2NUW"
SQ SEQUENCE 288 AA; 32516 MW; 131D33E25C9ACC78 CRC64;
MEIISPIITP FDKQGKVNVD ALKTHAKNLL EKGIDAIFVN GTTGLGPALS KDEKRQNLNA
LYDVTHKLIF QVGSLNLNDV MELVKFSNEM DILGVSSHSP YYFPRLPEKF LAKYYEEIAR
ISSHSLYIYN YPAATGYDIP PSILKSLPVK GIKDTNQDLA HSLEYKLNLP GVKVYNGSNT
LIYYSLLSLD GVVASFTNFI PEVIVKQRDL IKQGKLDDAL RLQELINRLA DILRKYGSIS
AIYVLVNEFQ GYDVGYPRPP IFPLTDEEAL SLKREIEPLK RKIQELVH
