ALF1_PYRAB
ID ALF1_PYRAB Reviewed; 281 AA.
AC Q9V2I6; G8ZFS3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=PYRAB00890; ORFNames=PAB0049;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB49012.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69464.1; -; Genomic_DNA.
DR PIR; E75195; E75195.
DR RefSeq; WP_010867213.1; NC_000868.1.
DR AlphaFoldDB; Q9V2I6; -.
DR SMR; Q9V2I6; -.
DR STRING; 272844.PAB0049; -.
DR EnsemblBacteria; CAB49012; CAB49012; PAB0049.
DR GeneID; 1494975; -.
DR KEGG; pab:PAB0049; -.
DR PATRIC; fig|272844.11.peg.102; -.
DR eggNOG; arCOG04044; Archaea.
DR HOGENOM; CLU_057069_2_2_2; -.
DR OMA; FVKVNYP; -.
DR OrthoDB; 36379at2157; -.
DR PhylomeDB; Q9V2I6; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Schiff base.
FT CHAIN 1..281
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000138948"
FT ACT_SITE 191
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 31222 MW; 6BFFCA8A4441D5A5 CRC64;
MEALQNIGIK RRLRRFFRRD GRALIFAMDH GFEHGPTDFE PVWEHVNPRV IIRKVVRAGV
DGVMMLPGMA RIAGDDVKPE VGLMIKITSK TNLRPKAEQL MQSQLAFVED AIKLGADAIA
ATVYWGSPQE DAMMRQFAEI VSYAHDLGFP VVQFAYPRGP YIDEKYGRKE DYRVVMYGAR
AAAEMGADMI KTYWTGSRET FAKVVDAAAG VPVLLSGGAK AENPLDFLKV VYEVIEAGGS
GAVVGRNIFQ RENPEPMIKA LIRVIHRNED PEEAAKAEGL L
