ID Q1JK26_STRPC Unreviewed; 293 AA.
AC Q1JK26;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013779};
GN Name=fba {ECO:0000313|EMBL:ABF32797.1};
GN OrderedLocusNames=MGAS9429_Spy1610 {ECO:0000313|EMBL:ABF32797.1};
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551 {ECO:0000313|EMBL:ABF32797.1, ECO:0000313|Proteomes:UP000002433};
RN [1] {ECO:0000313|EMBL:ABF32797.1, ECO:0000313|Proteomes:UP000002433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429 {ECO:0000313|EMBL:ABF32797.1,
RC ECO:0000313|Proteomes:UP000002433};
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
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DR EMBL; CP000259; ABF32797.1; -; Genomic_DNA.
DR RefSeq; WP_002988154.1; NC_008021.1.
DR AlphaFoldDB; Q1JK26; -.
DR KEGG; spk:MGAS9429_Spy1610; -.
DR HOGENOM; CLU_040088_0_1_9; -.
DR OMA; PRTWGKL; -.
DR Proteomes; UP000002433; 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:InterPro.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR011289; Fruc_bis_ald_class-2.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01859; fruc_bis_ald; 1.
DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 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.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABF32797.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 179
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 209..211
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 230..233
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 293 AA; 31222 MW; AD4304DDCE9F390D CRC64;
MAIVSAEKFV QAARENGYAV GGFNTNNLEW TQAILRAAEA KQAPVLIQTS MGAAKYMGGY
KVCQTLITNL VESMGITVPV AIHLDHGHYE DALECIEVGY TSIMFDGSHL PVEENLAKTA
EVVKIAHAKG VSVEAEVGTI GGEEDGIIGK GELAPIEDAK AMVETGIDFL AAGIGNIHGP
YPENWEGLAL DHLEKLTAAV PGFPIVLHGG SGIPDDQIKE AIRLGVAKVN VNTESQIAFS
NATREFARNY EANEAEYDGK KLFDPRKFLA PGMKAVQGAV EERIDVFGSA NKA
//