ID KBAY_ECOSM Reviewed; 286 AA.
AC B1LFP2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
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};
GN OrderedLocusNames=EcSMS35_3436;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB18539.1; -; Genomic_DNA.
DR RefSeq; WP_000022773.1; NC_010498.1.
DR AlphaFoldDB; B1LFP2; -.
DR SMR; B1LFP2; -.
DR KEGG; ecm:EcSMS35_3436; -.
DR HOGENOM; CLU_040088_0_1_6; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000007011; 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; Aldolase class I; 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 NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01858; tag_bisphos_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 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_0000355323"
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; 31338 MW; D71128F3819D4C3F CRC64;
MSIISTKYLL QDAQANGYAV PAFNIHNAET IQAILEVCSE MRSPVILAGT PGTFKHIALE
EIYALCSAYS TTYNMPLALH LDHHESLDDI RRKVHAGVRS AMIDGSHFPF DENVKLVKSV
VDFCHSQDCS VEAELGRLGG VEDDMSVDAE SAFLTDPQEA KRFVELTGVD SLAVAIGTAH
GLYSKTPKID FQRLAEIREV VDVPLVLHGA SDVPDEFVRR TIELGVTKVN VATELKIAFA
GAVKAWFAEN PQGNDPRYYM RVGMDAMKEV VRNKINVCGS ANRISA
//
