ID   KDGA_SACS2              Reviewed;         308 AA.
AC   Q97U28;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
DE            EC=4.1.2.55 {ECO:0000269|PubMed:15869466};
GN   Name=eda; OrderedLocusNames=SSO3197;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=15869466; DOI=10.1042/bj20041711;
RA   Ahmed H., Ettema T.J., Tjaden B., Geerling A.C., van der Oost J.,
RA   Siebers B.;
RT   "The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic
RT   archaea: a re-evaluation.";
RL   Biochem. J. 390:529-540(2005).
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:15869466}.
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:15869466};
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:15869466};
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; AE006641; AAK43294.1; -; Genomic_DNA.
DR   PIR; G90504; G90504.
DR   AlphaFoldDB; Q97U28; -.
DR   SMR; Q97U28; -.
DR   STRING; 273057.SSO3197; -.
DR   EnsemblBacteria; AAK43294; AAK43294; SSO3197.
DR   KEGG; sso:SSO3197; -.
DR   PATRIC; fig|273057.12.peg.3300; -.
DR   eggNOG; arCOG04172; Archaea.
DR   HOGENOM; CLU_049343_5_1_2; -.
DR   InParanoid; Q97U28; -.
DR   OMA; VVPPVCT; -.
DR   PhylomeDB; Q97U28; -.
DR   BRENDA; 4.1.2.55; 6163.
DR   UniPathway; UPA00856; UER00829.
DR   Proteomes; UP000001974; 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:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IBA:GO_Central.
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..308
FT                   /note="2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-
FT                   deoxy-6-phosphogalactonate aldolase"
FT                   /id="PRO_0000422655"
FT   ACT_SITE        169
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            144
FT                   /note="Proton shuttle"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  34795 MW;  6A5DE1EFB91D3C80 CRC64;
     MGRQGNLEEL WCLRMPEIIT PIITPFTKDN RIDKEKLKIH AENLIRKGID KLFVNGTTGL
     GPSLSPEEKL ENLKAVYDVT NKIIFQVGGL NLDDAIRLAK LSKDFDIVGI ASYAPYYYPR
     MSEKHLVKYF KTLCEVSPHP VYLYNYPTAT GKDIDAKVAK EIGCFTGVKD TIENIIHTLD
     YKRLNPNMLV YSGSDMLIAT VASTGLDGNV AAGSNYLPEV TVTIKKLAME RKIDEALKLQ
     FLHDEVIEAS RIFGSLSSNY VLTKYFQGYD LGYPRPPIFP LDDEEERQLI KKVEGIRAKL
     VELKILKE