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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
 
 
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