KBAY_ECO27
ID KBAY_ECO27 Reviewed; 286 AA.
AC B7UJ37;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit KbaY {ECO:0000255|HAMAP-Rule:MF_01293};
DE Short=TBPA {ECO:0000255|HAMAP-Rule:MF_01293};
DE Short=TagBP aldolase {ECO:0000255|HAMAP-Rule:MF_01293};
DE EC=4.1.2.40 {ECO:0000255|HAMAP-Rule:MF_01293};
DE AltName: Full=D-tagatose-bisphosphate aldolase class II {ECO:0000255|HAMAP-Rule:MF_01293};
DE AltName: Full=Ketose 1,6-bisphosphate aldolase class II {ECO:0000255|HAMAP-Rule:MF_01293};
DE AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000255|HAMAP-Rule:MF_01293};
GN Name=kbaY {ECO:0000255|HAMAP-Rule:MF_01293}; OrderedLocusNames=E2348C_3423;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase
CC KbaYZ, which catalyzes the reversible aldol condensation of
CC dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with
CC glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate
CC (TBP). Requires KbaZ subunit for full activity and stability.
CC {ECO:0000255|HAMAP-Rule:MF_01293}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:22948,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:58694, ChEBI:CHEBI:59776; EC=4.1.2.40;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01293};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01293};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01293};
CC -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation;
CC D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-
CC phosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01293}.
CC -!- SUBUNIT: Homotetramer. Forms a complex with KbaZ. {ECO:0000255|HAMAP-
CC Rule:MF_01293}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. TagBP aldolase KbaY subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01293}.
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DR EMBL; FM180568; CAS10971.1; -; Genomic_DNA.
DR RefSeq; WP_000022759.1; NC_011601.1.
DR AlphaFoldDB; B7UJ37; -.
DR SMR; B7UJ37; -.
DR EnsemblBacteria; CAS10971; CAS10971; E2348C_3423.
DR KEGG; ecg:E2348C_3423; -.
DR HOGENOM; CLU_040088_0_1_6; -.
DR OMA; PRTWGKL; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01293; TagBP_aldolase_KbaY; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR023788; TagBP_ald_KbaY.
DR InterPro; IPR011288; TagBP_ald_KbaY/GatY.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01858; tag_bisphos_ald; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Zinc.
FT CHAIN 1..286
FT /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaY"
FT /id="PRO_1000165275"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293"
FT BINDING 181
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293"
FT BINDING 209..211
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293"
FT BINDING 230..233
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01293"
SQ SEQUENCE 286 AA; 31367 MW; 9DAE17482B2129FC CRC64;
MSIISTKYLL QDAQANGYAV PAFNIHNAET IQAILEVCSE MRSPVILAGT PGTFKHIALE
EIYALCSAYS MTYNMPLALH LDHHESRDDI RRKVHAGVRS AMIDGSHFPF AENVKLVKSV
VDFCHSQDCS VEAELGRLGG VEDDMSVDAE SAFLTDPQEA KRFVELTGVD SLAVAIGTAH
GLYSKTPKID FQRLAEIREV VDVPLVLHGA SDVPDEFVRR TIELGVTKVN VATELKIAFA
GAVKAWFAEN PQGNDPRYYM RVGMDAMKEV VRNKINVCGS ANRISA
