ALF_STRR6
ID ALF_STRR6 Reviewed; 293 AA.
AC P0A4S2; O65944;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=fba; OrderedLocusNames=spr0530;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10387114; DOI=10.1007/pl00006823;
RA Jado I., Fenoll A., Cepeda T., Casal J., Perez A.;
RT "Cloning, sequencing, and chromosomal location of a putative class-II
RT aldolase gene from Streptococcus pneumoniae.";
RL Curr. Microbiol. 39:31-36(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [3]
RP PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15720398; DOI=10.1111/j.1742-4658.2005.04560.x;
RA Novakova L., Saskova L., Pallova P., Janecek J., Novotna J., Ulrych A.,
RA Echenique J., Trombe M.C., Branny P.;
RT "Characterization of a eukaryotic type serine/threonine protein kinase and
RT protein phosphatase of Streptococcus pneumoniae and identification of
RT kinase substrates.";
RL FEBS J. 272:1243-1254(2005).
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 -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15720398}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AJ005697; CAA06682.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99334.1; -; Genomic_DNA.
DR PIR; B97938; B97938.
DR RefSeq; NP_358124.1; NC_003098.1.
DR RefSeq; WP_001019003.1; NC_003098.1.
DR AlphaFoldDB; P0A4S2; -.
DR SMR; P0A4S2; -.
DR STRING; 171101.spr0530; -.
DR MoonProt; P0A4S2; -.
DR PRIDE; P0A4S2; -.
DR EnsemblBacteria; AAK99334; AAK99334; spr0530.
DR GeneID; 60233327; -.
DR GeneID; 66805762; -.
DR KEGG; spr:spr0530; -.
DR PATRIC; fig|171101.6.peg.582; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_9; -.
DR OMA; PRTWGKL; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000586; 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:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR011289; Fruc_bis_ald_class-2.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01859; fruc_bis_ald; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 1: Evidence at protein level;
KW Glycolysis; Lyase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..293
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178746"
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 209..211
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 230..233
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 31402 MW; 577D2A55713B6246 CRC64;
MAIVSAEKFV QAARDNGYAV GGFNTNNLEW TQAILRAAEA KKAPVLIQTS MGAAKYMGGY
KVARNLIANL VESMGITVPV AIHLDHGHYE DALECIEVGY TSIMFDGSHL PVEENLKLAK
EVVEKAHAKG ISVEAEVGTI GGEEDGIIGK GELAPIEDAK AMVETGIDFL AAGIGNIHGP
YPVNWEGLDL DHLQKLTEAL PGFPIVLHGG SGIPDEQIQA AIKLGVAKVN VNTECQIAFA
NATRKFARDY EANEAEYDKK KLFDPRKFLA DGVKAIQASV EERIDVFGSE GKA
