KBAY_ECOLI
ID KBAY_ECOLI Reviewed; 286 AA.
AC P0AB74; P42908; Q2M973;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
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, kba, yraC; OrderedLocusNames=b3137, JW3106;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP DISCUSSION OF SEQUENCE.
RX PubMed=8932697; DOI=10.1099/13500872-142-2-231;
RA Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr.;
RT "Novel phosphotransferase genes revealed by bacterial genome sequencing: a
RT gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in
RT Escherichia coli.";
RL Microbiology 142:231-250(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10712619; DOI=10.1046/j.1432-1327.2000.01191.x;
RA Zgiby S.M., Thomson G.J., Qamar S., Berry A.;
RT "Exploring substrate binding and discrimination in fructose 1,6-
RT bisphosphate and tagatose 1,6-bisphosphate aldolases.";
RL Eur. J. Biochem. 267:1858-1868(2000).
RN [5]
RP FUNCTION, AND COMPLEX WITH KBAZ.
RC STRAIN=K12;
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION
RP STATE ANALOG, AND ACTIVE SITE.
RX PubMed=11940603; DOI=10.1074/jbc.m202464200;
RA Hall D.R., Bond C.S., Leonard G.A., Watt C.I., Berry A., Hunter W.N.;
RT "Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral
RT discrimination, mechanism, and specificity of class II aldolases.";
RL J. Biol. Chem. 277:22018-22024(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.
CC {ECO:0000269|PubMed:10712619, 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 Evidence={ECO:0000269|PubMed:10712619};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for tagatose-1,6-bisphosphate
CC {ECO:0000269|PubMed:10712619};
CC KM=1.3 mM for fructose-1,6-bisphosphate
CC {ECO:0000269|PubMed:10712619};
CC Note=The catalytic efficiency measured with tagatose-1,6-bisphosphate
CC as substrate is 340-fold higher than that with fructose-1,6-
CC bisphosphate.;
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. Forms a complex with KbaZ.
CC {ECO:0000269|PubMed:10712619, ECO:0000269|PubMed:11940603}.
CC -!- INTERACTION:
CC P0AB74; P0A7K2: rplL; NbExp=2; IntAct=EBI-543669, EBI-543702;
CC -!- MASS SPECTROMETRY: Mass=31165.9; Mass_error=2.95; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10712619};
CC -!- MISCELLANEOUS: In contrast to E.coli strains C and EC3132, K-12 strains
CC cannot grow on N-acetylgalactosamine and D-galactosamine, because they
CC carry a deletion and thus lack active PTS systems specific for these
CC compounds. Therefore, KbaYZ in K-12 strains is not involved in the
CC degradation of these compounds.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. TagBP aldolase KbaY subfamily. {ECO:0000305}.
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DR EMBL; U18997; AAA57940.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76171.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77183.1; -; Genomic_DNA.
DR PIR; E65103; E65103.
DR RefSeq; NP_417606.1; NC_000913.3.
DR RefSeq; WP_000022766.1; NZ_STEB01000001.1.
DR PDB; 1GVF; X-ray; 1.45 A; A/B=1-286.
DR PDBsum; 1GVF; -.
DR AlphaFoldDB; P0AB74; -.
DR SMR; P0AB74; -.
DR BioGRID; 4261155; 23.
DR BioGRID; 851957; 1.
DR ComplexPortal; CPX-6022; KbaYZ tagatose-1,6-bisphosphate aldolase complex.
DR DIP; DIP-47961N; -.
DR IntAct; P0AB74; 7.
DR STRING; 511145.b3137; -.
DR DrugBank; DB03026; Phosphoglycolohydroxamic Acid.
DR PaxDb; P0AB74; -.
DR PRIDE; P0AB74; -.
DR EnsemblBacteria; AAC76171; AAC76171; b3137.
DR EnsemblBacteria; BAE77183; BAE77183; BAE77183.
DR GeneID; 66672962; -.
DR GeneID; 947644; -.
DR KEGG; ecj:JW3106; -.
DR KEGG; eco:b3137; -.
DR PATRIC; fig|1411691.4.peg.3593; -.
DR EchoBASE; EB2621; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_6; -.
DR InParanoid; P0AB74; -.
DR OMA; PRTWGKL; -.
DR PhylomeDB; P0AB74; -.
DR BioCyc; EcoCyc:TAGAALDOL1-MON; -.
DR BioCyc; MetaCyc:TAGAALDOL1-MON; -.
DR BRENDA; 4.1.2.40; 2026.
DR SABIO-RK; P0AB74; -.
DR UniPathway; UPA00704; UER00716.
DR EvolutionaryTrace; P0AB74; -.
DR PRO; PR:P0AB74; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902494; C:catalytic complex; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IC:ComplexPortal.
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 3D-structure; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..286
FT /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaY"
FT /id="PRO_0000178763"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:11940603"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11940603"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11940603"
FT BINDING 181
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11940603"
FT BINDING 209..211
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT BINDING 230..233
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1GVF"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:1GVF"
FT HELIX 256..278
FT /evidence="ECO:0007829|PDB:1GVF"
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
