ID   ALF1_PYRKO              Reviewed;         281 AA.
AC   Q8J308;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-biphosphate aldolase class I;
DE            Short=FBP aldolase;
DE   AltName: Full=Tk-fba;
GN   Name=fba; OrderedLocusNames=TK0989;
OS   Pyrococcus kodakaraensis (Thermococcus kodakaraensis).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KOD1;
RA   Imanaka H., Fukui T., Atomi H., Imanaka T.;
RT   "Fructose-1,6-bisphosphate aldolase from Thermococcus kodakaraensis
RT   KOD1.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=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
RT   Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT   genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- ENZYME REGULATION: Activated by citrate (By similarity).
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the deoC/fbaB aldolase family.
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DR   EMBL; AB083709; BAC21177.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD85178.1; -; Genomic_DNA.
DR   RefSeq; YP_183402.1; -.
DR   HSSP; P58315; 1OJX.
DR   GeneID; 3233691; -.
DR   GenomeReviews; AP006878_GR; TK0989.
DR   KEGG; tko:TK0989; -.
DR   NMPDR; fig|69014.3.peg.631; -.
DR   HOGENOM; Q8J308; -.
DR   OMA; Q8J308; VRHGHRG.
DR   BioCyc; TKOD69014:TK0989-MON; -.
DR   BRENDA; 4.1.2.13; 192130.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/AroFGH_arch.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01791; DeoC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; Lyase; Schiff base.
FT   CHAIN         1    281       Fructose-bisphosphate aldolase class 1.
FT                                /FTId=PRO_0000138951.
FT   ACT_SITE    191    191       Schiff-base intermediate with
FT                                dihydroxyacetone-P (By similarity).
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
//