位置:首页 > 蛋白库 > KBAY_ECOLU
KBAY_ECOLU
ID   KBAY_ECOLU              Reviewed;         286 AA.
AC   B7NDC5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=ECUMN_3621;
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR14775.1; -; Genomic_DNA.
DR   RefSeq; WP_000022773.1; NC_011751.1.
DR   RefSeq; YP_002414280.1; NC_011751.1.
DR   AlphaFoldDB; B7NDC5; -.
DR   SMR; B7NDC5; -.
DR   STRING; 585056.ECUMN_3621; -.
DR   EnsemblBacteria; CAR14775; CAR14775; ECUMN_3621.
DR   KEGG; eum:ECUMN_3621; -.
DR   PATRIC; fig|585056.7.peg.3801; -.
DR   HOGENOM; CLU_040088_0_1_6; -.
DR   OMA; PRTWGKL; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000007097; 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_1000140432"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024