ALF1_CLOB8
ID ALF1_CLOB8 Reviewed; 295 AA.
AC A6LXU8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Cbei_3039;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000721; ABR35178.1; -; Genomic_DNA.
DR RefSeq; WP_012059231.1; NC_009617.1.
DR AlphaFoldDB; A6LXU8; -.
DR SMR; A6LXU8; -.
DR STRING; 290402.Cbei_3039; -.
DR PRIDE; A6LXU8; -.
DR EnsemblBacteria; ABR35178; ABR35178; Cbei_3039.
DR KEGG; cbe:Cbei_3039; -.
DR eggNOG; COG3588; Bacteria.
DR HOGENOM; CLU_081560_0_0_9; -.
DR OMA; GVFGTKM; -.
DR OrthoDB; 945470at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000565; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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; Schiff base.
FT CHAIN 1..295
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_1000083323"
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; 33349 MW; 5576E1369D51F0EE CRC64;
MNENQMKRIH TGKGFIAALD QSGGSTPKAL LEYGIKENSY SNEDEMFGLV HEMRKRIIKS
PAFTLEYILG AILFEDTMYR TIDNQYTPDY LWKEKNIVPF LKVDKGLTEI ENGVQLMKPI
SNLDDLLKHA VEKNIFGTKM RSVIKEANAK GIKMLVNQQF EIGKQIVEAG LVPIIEPEVD
IHSTDKEESE KLLKLEILEQ LSKLDKETKV MLKLSIPTQD NFYIDLIDDP HVVRVVALSG
GYSQAEAKER LGRNHGLIAS FSRALSQGLT AQQTEEEFNG TISKSIKEIY EASIK
