KBAY_ECOLX
ID KBAY_ECOLX Reviewed; 286 AA.
AC Q9KIP8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit KbaY;
DE Short=TBPA;
DE Short=TagBP aldolase;
DE EC=4.1.2.40;
DE AltName: Full=D-tagatose-bisphosphate aldolase class II;
DE AltName: Full=Ketose 1,6-bisphosphate aldolase class II;
DE AltName: Full=Tagatose-bisphosphate aldolase;
GN Name=kbaY; Synonyms=agaY;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE CATABOLISM OF
RP N-ACETYLGALACTOSAMINE AND D-GALACTOSAMINE.
RC STRAIN=C;
RX PubMed=10931310; DOI=10.1046/j.1365-2958.2000.01969.x;
RA Brinkkoetter A., Kloess H., Alpert C.-A., Lengeler J.W.;
RT "Pathways for the utilization of N-acetyl-galactosamine and galactosamine
RT in Escherichia coli.";
RL Mol. Microbiol. 37:125-135(2000).
RN [2]
RP FUNCTION, AND COMPLEX WITH KBAZ.
RC STRAIN=C;
RX PubMed=11976750; DOI=10.1007/s00203-002-0406-6;
RA Brinkkoetter A., Shakeri-Garakani A., Lengeler J.W.;
RT "Two class II D-tagatose-bisphosphate aldolases from enteric bacteria.";
RL Arch. Microbiol. 177:410-419(2002).
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. Is
CC involved in the catabolism of N-acetylgalactosamine and D-
CC galactosamine. {ECO:0000269|PubMed:10931310,
CC ECO:0000269|PubMed:11976750}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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.
CC -!- SUBUNIT: Homotetramer (By similarity). Forms a complex with KbaZ.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. TagBP aldolase KbaY subfamily. {ECO:0000305}.
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DR EMBL; AF228498; AAF81089.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KIP8; -.
DR SMR; Q9KIP8; -.
DR STRING; 585034.ECIAI1_3287; -.
DR eggNOG; COG0191; Bacteria.
DR UniPathway; UPA00704; UER00716.
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 1: Evidence at protein level;
KW Lyase; Metal-binding; Zinc.
FT CHAIN 1..286
FT /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaY"
FT /id="PRO_0000355320"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 181
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_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 286 AA; 31245 MW; CAA42DF04A5AF68B 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 PQGNDPRNYM RVGMDAMKEV VRNKINVCGS ANRISA
