ALF1_PYRFU
ID ALF1_PYRFU Reviewed; 281 AA.
AC P58314;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=PF1956;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTAGENESIS OF
RP LYS-191.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11387336; DOI=10.1074/jbc.m103447200;
RA Siebers B., Brinkmann H., Doerr C., Tjaden B., Lilie H., van der Oost J.,
RA Verhees C.H.;
RT "Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of
RT archaeal type class I aldolases.";
RL J. Biol. Chem. 276:28710-28718(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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.
CC -!- SUBUNIT: Homooctamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR EMBL; AF368256; AAK83936.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL82080.1; -; Genomic_DNA.
DR RefSeq; WP_011013098.1; NC_018092.1.
DR AlphaFoldDB; P58314; -.
DR SMR; P58314; -.
DR STRING; 186497.PF1956; -.
DR EnsemblBacteria; AAL82080; AAL82080; PF1956.
DR GeneID; 41713778; -.
DR KEGG; pfu:PF1956; -.
DR PATRIC; fig|186497.12.peg.2029; -.
DR eggNOG; arCOG04044; Archaea.
DR HOGENOM; CLU_057069_2_2_2; -.
DR OMA; FVKVNYP; -.
DR OrthoDB; 36379at2157; -.
DR PhylomeDB; P58314; -.
DR BioCyc; MetaCyc:MON-11810; -.
DR BRENDA; 4.1.2.13; 5243.
DR SABIO-RK; P58314; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..281
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000138949"
FT ACT_SITE 191
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT MUTAGEN 191
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11387336"
SQ SEQUENCE 281 AA; 31135 MW; 19637AD0DA8CBD2F CRC64;
MEAPQNVGIK RRLKRFFRRD GRALIFAMDH GFEHGPTDFE PVWEHVNPRV IIRKVVRAGI
DGVMMLPGLA RIAGDEVKPE VGLMIKLTSK TNLRPKPEQL LQSQLGFVDD AIKLGADAIA
ATVYWGSPQE DVMMRQFAEI VSYAHDLGYP VVQFAYPRGP YIDEKYGKKE DYRVVMYGAR
AAAESGADMI KTYWTGSKET FAKVVEAAAG VPVLLSGGAK TENPVDFLKV VWEVIEAGGA
GAVVGRNIFQ RENPEPMIKA LIRVIHRNED PEEAAKAEGL I
