ALF1_CLOAB
ID ALF1_CLOAB Reviewed; 295 AA.
AC Q97TN4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000255|HAMAP-Rule:MF_00729};
DE EC=4.1.2.13 {ECO:0000255|HAMAP-Rule:MF_00729};
DE AltName: Full=Fructose-bisphosphate aldolase class I;
DE Short=FBP aldolase {ECO:0000255|HAMAP-Rule:MF_00729};
GN Name=fda {ECO:0000255|HAMAP-Rule:MF_00729}; OrderedLocusNames=CA_P0064;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OG Plasmid pSOL1.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00729};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000255|HAMAP-Rule:MF_00729}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000255|HAMAP-Rule:MF_00729}.
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DR EMBL; AE001438; AAK76810.1; -; Genomic_DNA.
DR RefSeq; NP_149228.1; NC_001988.2.
DR RefSeq; WP_010890749.1; NC_001988.2.
DR AlphaFoldDB; Q97TN4; -.
DR SMR; Q97TN4; -.
DR EnsemblBacteria; AAK76810; AAK76810; CA_P0064.
DR GeneID; 45000296; -.
DR KEGG; cac:CA_P0064; -.
DR PATRIC; fig|272562.8.peg.64; -.
DR HOGENOM; CLU_081560_0_0_9; -.
DR OMA; GVFGTKM; -.
DR OrthoDB; 945470at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000814; Plasmid pSOL1.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd00949; FBP_aldolase_I_bact; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00729; FBP_aldolase_1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR InterPro; IPR023014; FBA_I_Gram+-type.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Plasmid; Reference proteome; Schiff base.
FT CHAIN 1..295
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000216899"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT ACT_SITE 213
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
SQ SEQUENCE 295 AA; 33505 MW; 75C866B87CB11551 CRC64;
MNETQMNRIS KDKGFIAALD QSGGSTPKAL LQYGIKENSY SNDEEMFNLV HEMRKRIIKS
TAFNSKYILG AILFENTMYR TIDHKYTADY LWNEKNIVPF LKIDKGLSEL ENGVQLMKPI
TNLDELLKAA IEKNIFGTKM RSFIKEANSK GIKMVVDQQF ELADKIANQG LVPIIEPEVD
IKSTDKEKSE ELLKLEISKH LSDLDKETKV MLKLSIPTKD NFYSDLMKDP HVVRIVALSG
GYSQSEANER LSRNNGLIAS FSRALSENLS IDQTDEEFNE TLSNSIKEIY EASIT
