KBAZ_ECOLX
ID KBAZ_ECOLX Reviewed; 426 AA.
AC P0C8K1; P42903; Q2M977;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=D-tagatose-1,6-bisphosphate aldolase subunit KbaZ;
GN Name=kbaZ; Synonyms=agaZ;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE CATABOLISM OF
RP N-ACETYLGALACTOSAMINE AND D-GALACTOSAMINE.
RC STRAIN=C;
RX PubMed=10931310; DOI=10.1046/j.1365-2958.2000.01969.x;
RA Brinkkoetter A., Kloess H., Alpert C.-A., Lengeler J.W.;
RT "Pathways for the utilization of N-acetyl-galactosamine and galactosamine
RT in Escherichia coli.";
RL Mol. Microbiol. 37:125-135(2000).
RN [2]
RP FUNCTION AS A TAGBP ALDOLASE COMPONENT, AND COMPLEX WITH KBAY.
RC STRAIN=C;
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).
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. Is involved in the catabolism of N-acetylgalactosamine and D-
CC galactosamine. {ECO:0000269|PubMed:10931310,
CC ECO:0000269|PubMed:11976750}.
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: Forms a complex with KbaY.
CC -!- SIMILARITY: Belongs to the GatZ/KbaZ family. KbaZ subfamily.
CC {ECO:0000305}.
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DR EMBL; AF228498; AAF81082.1; -; Genomic_DNA.
DR RefSeq; WP_000681920.1; NZ_WVVZ01000010.1.
DR AlphaFoldDB; P0C8K1; -.
DR SMR; P0C8K1; -.
DR STRING; 585034.ECIAI1_3280; -.
DR eggNOG; COG4573; Bacteria.
DR OMA; QRHFSYS; -.
DR OrthoDB; 395879at2; -.
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 1: Evidence at protein level;
FT CHAIN 1..426
FT /note="D-tagatose-1,6-bisphosphate aldolase subunit KbaZ"
FT /id="PRO_0000355361"
SQ SEQUENCE 426 AA; 47192 MW; FC97956E662EA939 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
PAKASALSQM VENYETLIFE AHSTDYQTPQ SLRQLVIDHF AILKVGPALT FALREALFSL
AAIEEELVPA KACSGLRQVL EDVMLDRPEY WQSHYHGDGN ARRLARGYSY SDRVRYYWPD
SQIDDAFAHL VRNLADSPIP LPLISQYLPL QYVKVRSGEL QPTPRELIIN HIQDILAQYH
TACEGQ