ID   ALF1_PYRHO              Reviewed;         281 AA.
AC   O57840;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 117.
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;
GN   Name=fba; OrderedLocusNames=PH0082;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA29151.1; -; Genomic_DNA.
DR   PIR; H71227; H71227.
DR   RefSeq; WP_010884202.1; NC_000961.1.
DR   AlphaFoldDB; O57840; -.
DR   SMR; O57840; -.
DR   STRING; 70601.gene:9376990; -.
DR   EnsemblBacteria; BAA29151; BAA29151; BAA29151.
DR   GeneID; 1443984; -.
DR   KEGG; pho:PH0082; -.
DR   eggNOG; arCOG04044; Archaea.
DR   OrthoDB; 6329at2157; -.
DR   Proteomes; UP000000752; 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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   NCBIfam; NF040816; Fbpase1_Arch; 1.
DR   PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR   PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..281
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000138950"
FT   ACT_SITE        191
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   281 AA;  31189 MW;  9AB0E4501E983068 CRC64;
     MEALQNLGIR RRLKRFFRRD GRALIFAMDH GFEHGPTDFE PVWEHVNPKV IIRKVVRAGI
     DGVMMLPGIA RIAGDEVKPD VGLMIKLTSK TNLRPKPDQL LQSQLAYVED AIKLGADAIA
     ATVYWGSPQE DTMIRQFAEI ASYAHDLGYP VVQFAYPRGP YIDEKYGKKE DYRVVMYGAR
     AAAESGADMI KTYWTGSKET FAKVVEAAAG VPVLMSGGAK TDNPLDFLKV VWEVIEAGGS
     GAVVGRNIFQ RENPESMIRA LIRVIHRNED PEEAAKAEGL I
//