ALF_SHIFL
ID ALF_SHIFL Reviewed; 359 AA.
AC P0AB73; P11604;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Fructose-bisphosphate aldolase class 2;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
DE AltName: Full=Fructose-bisphosphate aldolase class II;
GN Name=fbaA; OrderedLocusNames=SF2910, S3110;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44392.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18214.1; -; Genomic_DNA.
DR RefSeq; NP_708685.2; NC_004337.2.
DR RefSeq; WP_000034372.1; NZ_WPGW01000018.1.
DR AlphaFoldDB; P0AB73; -.
DR SMR; P0AB73; -.
DR STRING; 198214.SF2910; -.
DR PRIDE; P0AB73; -.
DR EnsemblBacteria; AAN44392; AAN44392; SF2910.
DR EnsemblBacteria; AAP18214; AAP18214; S3110.
DR GeneID; 1025905; -.
DR GeneID; 66673198; -.
DR KEGG; sfl:SF2910; -.
DR KEGG; sfx:S3110; -.
DR PATRIC; fig|198214.7.peg.3461; -.
DR HOGENOM; CLU_036923_0_0_6; -.
DR OrthoDB; 827430at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00946; FBP_aldolase_IIA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR PANTHER; PTHR30559; PTHR30559; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..359
FT /note="Fructose-bisphosphate aldolase class 2"
FT /id="PRO_0000178734"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 266..268
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 287..290
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 39147 MW; 7A076D9EA62FBEC4 CRC64;
MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA AKVKAPVIVQ
FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH YGVPVILHTD HCAKKLLPWI
DGLLDAGEKH FAATGKPLFS SHMIDLSEES LQENIEICSK YLERMSKIGM TLEIELGCTG
GEEDGVDNSH MDASALYTQP EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT
ILRDSQEYVS KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV
LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL
