ID   ALF1_THEKO              Reviewed;         281 AA.
AC   Q8J308;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-bisphosphate aldolase class I;
DE            Short=FBP aldolase;
DE   AltName: Full=Tk-fba;
GN   Name=fba; OrderedLocusNames=TK0989;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RA   Imanaka H., Fukui T., Atomi H., Imanaka T.;
RT   "Fructose-1,6-bisphosphate aldolase from Thermococcus kodakaraensis KOD1.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC   -!- ACTIVITY REGULATION: Activated by citrate. {ECO:0000250}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR   EMBL; AB083709; BAC21177.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85178.1; -; Genomic_DNA.
DR   RefSeq; WP_011249940.1; NC_006624.1.
DR   AlphaFoldDB; Q8J308; -.
DR   SMR; Q8J308; -.
DR   STRING; 69014.TK0989; -.
DR   EnsemblBacteria; BAD85178; BAD85178; TK0989.
DR   GeneID; 3233691; -.
DR   KEGG; tko:TK0989; -.
DR   PATRIC; fig|69014.16.peg.967; -.
DR   eggNOG; arCOG04044; Archaea.
DR   HOGENOM; CLU_057069_2_2_2; -.
DR   InParanoid; Q8J308; -.
DR   OMA; FVKVNYP; -.
DR   OrthoDB; 36379at2157; -.
DR   PhylomeDB; Q8J308; -.
DR   SABIO-RK; Q8J308; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..281
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000138951"
FT   ACT_SITE        191
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   281 AA;  31240 MW;  9A95B90F50324B79 CRC64;
     MDAYQSVGIR RRLKRFFRRD GRALIFAMDH GFEHGPTDFE PVWEHVNPRI IIRKVVRAGV
     DGVMMLPGIV RMAGDELKPD TGLMIKLTSK TELRPKEEQL LQSQLGYVED AIKLGADAIA
     ATVYWGSPQE DVMMRQFAEI ASYAHDLGFP VVQFAYPRGP YINEKYGKKE DYRVVMYGAR
     AAAETGADMI KTYWTGSKET FAKVVDAAAG VPVLLSGGAK TDNPVDFLKV VWDVIEAGGA
     GAVVGRNIFQ RENPEPMIKA LIRVIHRNED PEEAAKAEGL I