DGAF_SALT1
ID DGAF_SALT1 Reviewed; 247 AA.
AC D0ZLR2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase {ECO:0000303|PubMed:23836865};
DE EC=4.1.2.14 {ECO:0000269|PubMed:23836865};
DE AltName: Full=Keto-3-deoxygluconate 6-phosphate aldolase {ECO:0000303|PubMed:23836865};
DE Short=KDGP aldolase {ECO:0000303|PubMed:23836865};
GN Name=dgaF {ECO:0000303|PubMed:23836865}; OrderedLocusNames=STM14_4543;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=23836865; DOI=10.1128/jb.00290-13;
RA Miller K.A., Phillips R.S., Mrazek J., Hoover T.R.;
RT "Salmonella utilizes D-glucosaminate via a mannose family
RT phosphotransferase system permease and associated enzymes.";
RL J. Bacteriol. 195:4057-4066(2013).
CC -!- FUNCTION: Involved in the catabolism of D-glucosaminate. Catalyzes the
CC conversion of keto-3-deoxygluconate 6-phosphate (KDGP) to yield
CC pyruvate and glyceraldehyde-3-phosphate. {ECO:0000269|PubMed:23836865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3-
CC phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.14;
CC Evidence={ECO:0000269|PubMed:23836865};
CC -!- INDUCTION: By D-glucosaminate and DgaR. {ECO:0000269|PubMed:23836865}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are able to grow with D-
CC glucosaminate as the sole carbon source, although the growth rate is
CC significantly lower. {ECO:0000269|PubMed:23836865}.
CC -!- SIMILARITY: Belongs to the DagF family. {ECO:0000305}.
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DR EMBL; CP001363; ACY90924.1; -; Genomic_DNA.
DR RefSeq; WP_001186146.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZLR2; -.
DR SMR; D0ZLR2; -.
DR EnsemblBacteria; ACY90924; ACY90924; STM14_4543.
DR KEGG; seo:STM14_4543; -.
DR PATRIC; fig|588858.6.peg.4141; -.
DR HOGENOM; CLU_098610_0_0_6; -.
DR OMA; GGHAAKF; -.
DR BioCyc; MetaCyc:MON-18125; -.
DR BioCyc; SENT588858:STM14_RS19900-MON; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0008675; F:2-dehydro-3-deoxy-phosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010763; DgaF.
DR Pfam; PF07071; KDGP_aldolase; 1.
DR TIGRFAMs; TIGR03581; EF_0839; 1.
PE 1: Evidence at protein level;
KW Lyase.
FT CHAIN 1..247
FT /note="2-dehydro-3-deoxy-phosphogluconate aldolase"
FT /id="PRO_0000430795"
SQ SEQUENCE 247 AA; 25896 MW; AA091A6B785462B0 CRC64;
MQQINFYRQR VAINVLAKDI ANAKAIYEAA EGHAVIGVLS AQFATVEEGV PEVKRWMAEV
PSISVGLGAG DPAQYYKAAM IAAHTHPAHV NQTFTGSGFA AGALAATGGE QTHINALVSP
TGTPGEVVIS TGVSSSQGTP ARVSCEAAVR MMQDMGAHAA KFFPMGGEKS LPELYALATT
AARHGMTLIE PTGGISLDNF GIILQTCLEA GVPRVMPHVY SSIIDPQTGN TRPEDIIRLM
EIVKALV
