KBAZ_ECO5E
ID KBAZ_ECO5E Reviewed; 426 AA.
AC B5YS22;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit KbaZ {ECO:0000255|HAMAP-Rule:MF_01295};
GN Name=kbaZ {ECO:0000255|HAMAP-Rule:MF_01295};
GN OrderedLocusNames=ECH74115_4446;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
CC -!- FUNCTION: Component of the tagatose-1,6-bisphosphate aldolase KbaYZ
CC that is required for full activity and stability of the Y subunit.
CC Could have a chaperone-like function for the proper and stable folding
CC of KbaY. When expressed alone, KbaZ does not show any aldolase
CC activity. {ECO:0000255|HAMAP-Rule:MF_01295}.
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_01295}.
CC -!- SUBUNIT: Forms a complex with KbaY. {ECO:0000255|HAMAP-Rule:MF_01295}.
CC -!- SIMILARITY: Belongs to the GatZ/KbaZ family. KbaZ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01295}.
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; CP001164; ACI37126.1; -; Genomic_DNA.
DR RefSeq; WP_000681927.1; NC_011353.1.
DR AlphaFoldDB; B5YS22; -.
DR SMR; B5YS22; -.
DR KEGG; ecf:ECH74115_4446; -.
DR HOGENOM; CLU_053334_0_0_6; -.
DR OMA; QRHFSYS; -.
DR UniPathway; UPA00704; UER00716.
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_01295; Tagatose_aldol_KbaZ; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012062; GatZ/KbaZ-like.
DR InterPro; IPR023435; TagBP_ald_KbaZ.
DR Pfam; PF08013; GatZ_KbaZ-like; 1.
DR PIRSF; PIRSF009264; TagBP_ald_AgaZ; 1.
DR TIGRFAMs; TIGR02810; agaZ_gatZ; 1.
PE 3: Inferred from homology;
FT CHAIN 1..426
FT /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaZ"
FT /id="PRO_0000372533"
SQ SEQUENCE 426 AA; 47177 MW; 60D851E04B72426F CRC64;
MKHLTEMVRQ HKAGKTNGIY AVCSAHPLVL EAAIRYASAN QTPLLIEATS NQVDQFGGYT
GMTPADFRGF VCQLADSLNF PQDALILGGD HLGPNRWQNL PAAQAMANAD DLIKSYVAAG
FKKIHLDCSM SCQDDPIPLT DDIVAERAAR LAKVAEETCL EHFGEADLEY VIGTEVPVPG
GAHETLSELA VTTPDAARAT LEAHRHAFEK QGLNAIWPRI IALVVQPGVE FDHTNVIDYQ
PAKATALSQM VESYETLIFE AHSTDYQTPQ SLRQLVIDHF AILKVGPALT FALREALFSL
AAIEEELVPA KACSGLRQVL ENVMLNRPEY WQSHYHGDGN ARRLARGYSY SDRVRYYWPD
SQIDDAFAHL VRNLADSPIP LPLISQYLPL QYVKVRSGEL QPTPRELIIN HIQDILAQYH
TACEGQ