ID   ALF_ECOLI               Reviewed;         359 AA.
AC   P0AB71; P11604; Q2M9R7;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 153.
DE   RecName: Full=Fructose-bisphosphate aldolase class 2;
DE            Short=FBP aldolase;
DE            Short=FBPA;
DE            EC=4.1.2.13 {ECO:0000269|PubMed:10712619};
DE   AltName: Full=Fructose-1,6-bisphosphate aldolase;
DE   AltName: Full=Fructose-bisphosphate aldolase class II;
DE   AltName: Full=Sedoheptulose bisphosphate aldolase {ECO:0000305};
GN   Name=fbaA; Synonyms=fba, fda; OrderedLocusNames=b2925, JW2892;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / CS520;
RX   PubMed=2546007; DOI=10.1111/j.1365-2958.1989.tb00221.x;
RA   Alefounder P.R., Perham R.N.;
RT   "Identification, molecular cloning and sequence analysis of a gene cluster
RT   encoding the class II fructose 1,6-bisphosphate aldolase, 3-
RT   phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate
RT   dehydrogenase of Escherichia coli.";
RL   Mol. Microbiol. 3:723-732(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-27.
RX   PubMed=2649077; DOI=10.1042/bj2570529;
RA   Alefounder P.R., Baldwin S.A., Perham R.N., Short N.J.;
RT   "Cloning, sequence analysis and over-expression of the gene for the class
RT   II fructose 1,6-bisphosphate aldolase of Escherichia coli.";
RL   Biochem. J. 257:529-534(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-5.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA   Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA   Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA   Hochstrasser D.F.;
RT   "Protein identification with N and C-terminal sequence tags in proteome
RT   projects.";
RL   J. Mol. Biol. 278:599-608(1998).
RN   [7]
RP   MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112.
RX   PubMed=8436219; DOI=10.1016/0014-5793(93)81317-s;
RA   Berry A., Marshall K.E.;
RT   "Identification of zinc-binding ligands in the class II fructose-1,6-
RT   bisphosphate aldolase of Escherichia coli.";
RL   FEBS Lett. 318:11-16(1993).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP   REACTION MECHANISM, AND MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=10712619; DOI=10.1046/j.1432-1327.2000.01191.x;
RA   Zgiby S.M., Thomson G.J., Qamar S., Berry A.;
RT   "Exploring substrate binding and discrimination in fructose 1,6-
RT   bisphosphate and tagatose 1,6-bisphosphate aldolases.";
RL   Eur. J. Biochem. 267:1858-1868(2000).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
RN   [10]
RP   FUNCTION IN SEDOHEPTULOSE BISPHOSPHATE BYPASS PATHWAY, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=K12 / BW25113;
RX   PubMed=19756045; DOI=10.1038/msb.2009.65;
RA   Nakahigashi K., Toya Y., Ishii N., Soga T., Hasegawa M., Watanabe H.,
RA   Takai Y., Honma M., Mori H., Tomita M.;
RT   "Systematic phenome analysis of Escherichia coli multiple-knockout mutants
RT   reveals hidden reactions in central carbon metabolism.";
RL   Mol. Syst. Biol. 5:306-306(2009).
RN   [11]
RP   MALONYLATION AT LYS-9.
RC   STRAIN=K12;
RX   PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA   Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA   Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA   Verdin E., Ye Y., Zhao Y.;
RT   "The first identification of lysine malonylation substrates and its
RT   regulatory enzyme.";
RL   Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN   [12]
RP   SUCCINYLATION AT LYS-9; LYS-72; LYS-115; LYS-231; LYS-251; LYS-319; LYS-326
RP   AND LYS-348.
RC   STRAIN=K12;
RX   PubMed=21151122; DOI=10.1038/nchembio.495;
RA   Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
RT   "Identification of lysine succinylation as a new post-translational
RT   modification.";
RL   Nat. Chem. Biol. 7:58-63(2011).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=8836102; DOI=10.1038/nsb1096-856;
RA   Blom N.S., Tetreault S., Coulombe R., Sygusch J.;
RT   "Novel active site in Escherichia coli fructose 1,6-bisphosphate
RT   aldolase.";
RL   Nat. Struct. Biol. 3:856-862(1996).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=8939754; DOI=10.1016/s0969-2126(96)00138-4;
RA   Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W., Naismith J.H.,
RA   Qamar S., Plater A., Berry A., Hunter W.N.;
RT   "The crystal structure of a class II fructose-1,6-bisphosphate aldolase
RT   shows a novel binuclear metal-binding active site embedded in a familiar
RT   fold.";
RL   Structure 4:1303-1315(1996).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION
RP   STATE ANALOG, AND ACTIVE SITE.
RX   PubMed=10080900; DOI=10.1006/jmbi.1999.2609;
RA   Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., Hunter W.N.;
RT   "The crystal structure of Escherichia coli class II fructose-1, 6-
RT   bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals
RT   details of mechanism and specificity.";
RL   J. Mol. Biol. 287:383-394(1999).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM, AND METAL
RP   BINDING SITES.
RX   PubMed=12595741; DOI=10.1107/s0907444902023661;
RA   Hall D.R., Kemp L.E., Leonard G.A., Marshall K., Berry A., Hunter W.N.;
RT   "The organization of divalent cations in the active site of cadmium
RT   Escherichia coli fructose-1,6-bisphosphate aldolase.";
RL   Acta Crystallogr. D 59:611-614(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 (PubMed:10712619). In addition, is
CC       involved in the utilization of D-sedoheptulose 7-phosphate, an
CC       intermediate of the pentose phosphate pathway, via the sedoheptulose
CC       bisphosphate bypass pathway (PubMed:19756045). Catalyzes the cleavage
CC       of D-sedoheptulose 1,7-bisphosphate to glyceraldehyde 3-phosphate and
CC       erythrose 4-phosphate (PubMed:19756045). {ECO:0000269|PubMed:10712619,
CC       ECO:0000269|PubMed:19756045}.
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:0000269|PubMed:10712619};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + dihydroxyacetone phosphate = D-
CC         sedoheptulose 1,7-bisphosphate; Xref=Rhea:RHEA:30167,
CC         ChEBI:CHEBI:16897, ChEBI:CHEBI:57642, ChEBI:CHEBI:58335;
CC         Evidence={ECO:0000269|PubMed:19756045};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30169;
CC         Evidence={ECO:0000269|PubMed:19756045};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102,
CC         ECO:0000269|PubMed:8939754};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC       provides a structural contribution. {ECO:0000269|PubMed:10080900,
CC       ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.17 mM for fructose-1,6-bisphosphate
CC         {ECO:0000269|PubMed:10712619};
CC         KM=0.35 mM for tagatose-1,6-bisphosphate
CC         {ECO:0000269|PubMed:10712619};
CC         Note=The catalytic efficiency measured with fructose-1,6-bisphosphate
CC         as substrate is 1440-fold higher than that with
CC         tagatose-1,6-bisphosphate.;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10080900,
CC       ECO:0000269|PubMed:12595741, ECO:0000269|PubMed:8836102,
CC       ECO:0000269|PubMed:8939754}.
CC   -!- INTERACTION:
CC       P0AB71; P0A6Y8: dnaK; NbExp=3; IntAct=EBI-370916, EBI-542092;
CC       P0AB71; P0AB71: fbaA; NbExp=4; IntAct=EBI-370916, EBI-370916;
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; X14436; CAA32605.1; -; Genomic_DNA.
DR   EMBL; U28377; AAA69092.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75962.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76989.1; -; Genomic_DNA.
DR   PIR; S02177; ADEC2A.
DR   RefSeq; NP_417400.1; NC_000913.3.
DR   RefSeq; WP_000034372.1; NZ_CP009789.1.
DR   PDB; 1B57; X-ray; 2.00 A; A/B=2-359.
DR   PDB; 1DOS; X-ray; 1.67 A; A/B=2-359.
DR   PDB; 1GYN; X-ray; 2.00 A; A=2-359.
DR   PDB; 1ZEN; X-ray; 2.50 A; A=2-359.
DR   PDB; 5GK3; X-ray; 1.80 A; A/B=1-359.
DR   PDB; 5GK4; X-ray; 2.00 A; A/B=1-359.
DR   PDB; 5GK5; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-359.
DR   PDB; 5GK6; X-ray; 1.80 A; A/B=1-359.
DR   PDB; 5GK7; X-ray; 1.80 A; A/B=1-359.
DR   PDB; 5GK8; X-ray; 2.00 A; A/B=1-359.
DR   PDB; 5VJD; X-ray; 1.70 A; A/B=2-359.
DR   PDB; 5VJE; X-ray; 1.65 A; A/B=2-359.
DR   AlphaFoldDB; P0AB71; -.
DR   MDRepo; P0AB71; -.
DR   SMR; P0AB71; -.
DR   BioGRID; 4262069; 20.
DR   BioGRID; 851736; 2.
DR   DIP; DIP-31872N; -.
DR   FunCoup; P0AB71; 586.
DR   IntAct; P0AB71; 7.
DR   STRING; 511145.b2925; -.
DR   BindingDB; P0AB71; -.
DR   ChEMBL; CHEMBL4912; -.
DR   DrugBank; DB03026; Phosphoglycolohydroxamic Acid.
DR   iPTMnet; P0AB71; -.
DR   jPOST; P0AB71; -.
DR   PaxDb; 511145-b2925; -.
DR   EnsemblBacteria; AAC75962; AAC75962; b2925.
DR   GeneID; 93779073; -.
DR   GeneID; 947415; -.
DR   KEGG; ecj:JW2892; -.
DR   KEGG; eco:b2925; -.
DR   KEGG; ecoc:C3026_16025; -.
DR   PATRIC; fig|1411691.4.peg.3807; -.
DR   EchoBASE; EB0278; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_036923_0_0_6; -.
DR   InParanoid; P0AB71; -.
DR   OMA; HIDFVFH; -.
DR   OrthoDB; 9803995at2; -.
DR   PhylomeDB; P0AB71; -.
DR   BioCyc; EcoCyc:FRUCTBISALD-CLASSII-MONOMER; -.
DR   BioCyc; MetaCyc:FRUCTBISALD-CLASSII-MONOMER; -.
DR   BRENDA; 4.1.2.13; 2026.
DR   SABIO-RK; P0AB71; -.
DR   UniPathway; UPA00109; UER00183.
DR   EvolutionaryTrace; P0AB71; -.
DR   PRO; PR:P0AB71; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P0AB71; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
DR   CDD; cd00946; FBP_aldolase_IIA; 1.
DR   DisProt; DP03662; -.
DR   FunFam; 3.20.20.70:FF:000013; Class II fructose-bisphosphate aldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006411; Fruct_bisP_bact.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01520; FruBisAldo_II_A; 1.
DR   NCBIfam; NF006628; PRK09197.1; 1.
DR   PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
DR   PDBsum; 1B57; -.
DR   PDBsum; 1DOS; -.
DR   PDBsum; 1GYN; -.
DR   PDBsum; 1ZEN; -.
DR   PDBsum; 5GK3; -.
DR   PDBsum; 5GK4; -.
DR   PDBsum; 5GK5; -.
DR   PDBsum; 5GK6; -.
DR   PDBsum; 5GK7; -.
DR   PDBsum; 5GK8; -.
DR   PDBsum; 5VJD; -.
DR   PDBsum; 5VJE; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Glycolysis; Lyase;
KW   Metal-binding; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2649077,
FT                   ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841"
FT   CHAIN           2..359
FT                   /note="Fructose-bisphosphate aldolase class 2"
FT                   /id="PRO_0000178713"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:10080900"
FT   BINDING         62
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000305"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:10080900,
FT                   ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10080900,
FT                   ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10080900,
FT                   ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:10080900,
FT                   ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT   BINDING         228
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:10080900,
FT                   ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754"
FT   BINDING         266..268
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT   BINDING         287..290
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT   MOD_RES         9
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MOD_RES         9
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21908771"
FT   MOD_RES         9
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         72
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         115
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         231
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         251
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         319
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         326
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MOD_RES         348
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000269|PubMed:21151122"
FT   MUTAGEN         36
FT                   /note="N->A: 1.5% of wild-type activity. 5-fold decrease in
FT                   FBP affinity."
FT                   /evidence="ECO:0000269|PubMed:10712619"
FT   MUTAGEN         60
FT                   /note="Q->A: 81% of wild-type activity. 1.3-fold decrease
FT                   in FBP affinity."
FT                   /evidence="ECO:0000269|PubMed:10712619"
FT   MUTAGEN         62
FT                   /note="S->A: 8% of wild-type activity. 16-fold decrease in
FT                   FBP affinity."
FT                   /evidence="ECO:0000269|PubMed:10712619"
FT   MUTAGEN         62
FT                   /note="S->T: 60% of wild-type activity. 2.5-fold decrease
FT                   in FBP affinity."
FT                   /evidence="ECO:0000269|PubMed:10712619"
FT   MUTAGEN         108
FT                   /note="H->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8436219"
FT   MUTAGEN         111
FT                   /note="H->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8436219"
FT   MUTAGEN         112
FT                   /note="C->A: Partial loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8436219"
FT   MUTAGEN         326
FT                   /note="K->A: 6% of wild-type activity. 2.2-fold decrease in
FT                   FBP affinity."
FT                   /evidence="ECO:0000269|PubMed:10712619"
FT   HELIX           4..7
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           40..53
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           63..70
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           81..101
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           117..134
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          140..144
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           151..166
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           200..211
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          217..221
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:5VJD"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:1ZEN"
FT   HELIX           240..253
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           272..280
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          283..288
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           290..306
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          311..317
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   STRAND          320..324
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           326..329
FT                   /evidence="ECO:0007829|PDB:5VJE"
FT   HELIX           331..352
FT                   /evidence="ECO:0007829|PDB:5VJE"
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
//