ALF1_ECOL6
ID ALF1_ECOL6 Reviewed; 350 AA.
AC P0A992; P71295; P76416;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 84.
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=fbaB; OrderedLocusNames=c2623;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 -!- SUBUNIT: Homooctamer or homodecamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. FbaB subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN81079.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN81079.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000129551.1; NC_004431.1.
DR AlphaFoldDB; P0A992; -.
DR SMR; P0A992; -.
DR STRING; 199310.c2623; -.
DR EnsemblBacteria; AAN81079; AAN81079; c2623.
DR GeneID; 66674007; -.
DR KEGG; ecc:c2623; -.
DR eggNOG; COG1830; Bacteria.
DR HOGENOM; CLU_057069_0_0_6; -.
DR OMA; FVKVNYP; -.
DR Proteomes; UP000001410; 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 SMART; SM01133; DeoC; 1.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Glycolysis; Lyase; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..350
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000138940"
FT ACT_SITE 237
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT MOD_RES 208
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 38109 MW; 462341BE2459E587 CRC64;
MTDIAQLLGK DADNLLQHRC MTIPSDQLYL PGHDYVDRVM IDNNRPPAVL RNMQTLYNTG
RLAGTGYLSI LPVDQGVEHS AGASFAANPL YFDPKNIVEL AIEAGCNCVA STYGVLASVS
RRYAHRIPFL VKLNHNETLS YPNTYDQTLY ASVEQAFNMG AVAVGATIYF GSEESRRQIE
EISAAFERAH ELGMVTVLWA YLRNSAFKKD GVDYHVSADL TGQANHLAAT IGADIVKQKM
AENNGGYKAI NYGYTDDRVY SKLTSENPID LVRYQLANCY MGRAGLINSG GAAGGETDLS
DAVRTAVINK RAGGMGLILG RKAFKKSMAD GVKLINAVQD VYLDSKITIA
