ID   KBAZ_ECOK1              Reviewed;         426 AA.
AC   A1AG39;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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}; Synonyms=agaZ;
GN   OrderedLocusNames=Ecok1_31350; ORFNames=APECO1_3297;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ02629.1; -; Genomic_DNA.
DR   RefSeq; WP_000681931.1; NC_008563.1.
DR   AlphaFoldDB; A1AG39; -.
DR   SMR; A1AG39; -.
DR   EnsemblBacteria; ABJ02629; ABJ02629; APECO1_3297.
DR   KEGG; ecv:APECO1_3297; -.
DR   HOGENOM; CLU_053334_0_0_6; -.
DR   OMA; QRHFSYS; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000008216; Chromosome.
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_0000372535"
SQ   SEQUENCE   426 AA;  47218 MW;  92DD6B4128A967E7 CRC64;
     MKHLTEMVRQ HKAGKTNGIY AVCSAHPLVL EAAIRYASAN QTPLLIEATS NQVDQFGGYT
     GMTPADFRGF VCQLADSLNF PQDALILGGD HLGPNRWQNL PAAQAMANAD DLIKSYVAAG
     FKKIHLDCSM SCQDDPIPLT DDIVAERAAR LAKVAEETCR EHFGEADLEY VIGTEVPVPG
     GAHETLSELA VTTPDAARAT LEAHRHAFEK QGLNAIWPRI IALVVQPGVE FDHTNVIDYQ
     PAKAAALSQM VENYETLIFE AHSTDYQTPQ SLRQLVIDHF AILKVGPALT FALREALFSL
     AAIEEELVPA KACSGLRQVL ENVMLDRPEY WQSHYHGDGN ARRLARGYSY SDRVRYYWPD
     SQIDDAFAHL VRNLADSPIP LPLISQYLPL QYVKVRSGEL QPTPRELIIN HIQDILAQYH
     TACEGQ