ID   KBAZ_CITK8              Reviewed;         431 AA.
AC   A8AQ21;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 79.
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}; OrderedLocusNames=CKO_04530;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABV15584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000822; ABV15584.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024130977.1; NC_009792.1.
DR   AlphaFoldDB; A8AQ21; -.
DR   SMR; A8AQ21; -.
DR   STRING; 290338.CKO_04530; -.
DR   EnsemblBacteria; ABV15584; ABV15584; CKO_04530.
DR   GeneID; 45138081; -.
DR   KEGG; cko:CKO_04530; -.
DR   HOGENOM; CLU_053334_0_0_6; -.
DR   OrthoDB; 395879at2; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000008148; 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;
KW   Reference proteome.
FT   CHAIN           1..431
FT                   /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaZ"
FT                   /id="PRO_0000372522"
SQ   SEQUENCE   431 AA;  47978 MW;  C631B84B1D23CF9A CRC64;
     MKHLTEMVEQ HKRGNTNGIY AVCSAHPLVL EAAIRYAHAN HTPLLIEATS NQVDQFGGYT
     GMTPADFRGF VYQLADSLNF PQSQLILGGD HLGPNRWQNL PAAQAMANAD DLIKSYVAAG
     FKKIHLDCSM SCANDPIPLT DEIVAERAAR LAKIAEETCR EHFGESDLVY VIGTEVPVPG
     GAHETLTELE VTTPDAARAT LEAHRHAFEK QGLSAIWPRI IGLVVQPGVE FDHTHIIDYQ
     PQKAIALSAM VEAYDTLVFE AHSTDYQTPQ SLRQLVKDHF AILKVGPALT FALREALFSL
     AAIEEELLPA KTSSGLRHVL ESVMLDRPEY WQSHYHGDGN ARRLARGYSY SDRVRYYWPD
     QQIDEAFARL VRNLADDPIP LPLISQYLPL QYARVREGDL NATPRELIIS HIQDVLQQYH
     AACQGVTSQN A