KBAY_ENT38
ID KBAY_ENT38 Reviewed; 292 AA.
AC A4WEV6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Ent638_3578;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000653; ABP62236.1; -; Genomic_DNA.
DR RefSeq; WP_015960562.1; NC_009436.1.
DR AlphaFoldDB; A4WEV6; -.
DR SMR; A4WEV6; -.
DR STRING; 399742.Ent638_3578; -.
DR EnsemblBacteria; ABP62236; ABP62236; Ent638_3578.
DR KEGG; ent:Ent638_3578; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_6; -.
DR OMA; NNMEIVQ; -.
DR OrthoDB; 827430at2; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000000230; 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..292
FT /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaY"
FT /id="PRO_0000355319"
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 292 AA; 32127 MW; 988B914818B065C5 CRC64;
MSIISTKYLL QDAQAKGYAV PAFNIHNAET IQAILEVCSE MRSPVILAGT PGTFKHIALE
EIYALCSAYS ISYDMPLALH LDHHESLDDI RRKVNAGVRS AMIDGSHFPF EQNVTLVKSV
VDFCHLNDCS VEAELGRLGG MEDDMSVDAE SAFLTDPQEA KRFVELTGVD SLAVAIGTAH
GLYTKRPKID FQRLAEIRDV VDIPLVLHGA SDVPDEFVRR TIELGVCKVN VATELKIAFS
AAVKEWFNEN PQGNDPRFYM RVGMDAMKEV VKNKINVCGS ANKLVLDSAV VL
