KBAY_ECOL5
ID KBAY_ECOL5 Reviewed; 286 AA.
AC Q0TCW8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=ECP_3229;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG71211.1; -; Genomic_DNA.
DR RefSeq; WP_000022766.1; NC_008253.1.
DR AlphaFoldDB; Q0TCW8; -.
DR SMR; Q0TCW8; -.
DR STRING; 362663.ECP_3229; -.
DR EnsemblBacteria; ABG71211; ABG71211; ECP_3229.
DR GeneID; 66672962; -.
DR KEGG; ecp:ECP_3229; -.
DR HOGENOM; CLU_040088_0_1_6; -.
DR OMA; PRTWGKL; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000009182; 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_0000355327"
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; 31294 MW; CAA42DF05C2B918B CRC64;
MSIISTKYLL QDAQANGYAV PAFNIHNAET IQAILEVCSE MRSPVILAGT PGTFKHIALE
EIYALCSAYS TTYNMPLALH LDHHESLDDI RRKVHAGVRS AMIDGSHFPF AENVKLVKSV
VDFCHSQDCS VEAELGRLGG VEDDMSVDAE SAFLTDPQEA KRFVELTGVD SLAVAIGTAH
GLYSKTPKID FQRLAEIREV VDVPLVLHGA SDVPDEFVRR TIELGVTKVN VATELKIAFA
GAVKAWFAEN PQGNDPRYYM RVGMDAMKEV VRNKINVCGS ANRISA
