YDFG_SALTY
ID YDFG_SALTY Reviewed; 248 AA.
AC P69936; P40864;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=NADP-dependent 3-hydroxy acid dehydrogenase YdfG {ECO:0000250|UniProtKB:P39831};
DE AltName: Full=L-allo-threonine dehydrogenase {ECO:0000250|UniProtKB:P39831};
DE EC=1.1.1.381 {ECO:0000250|UniProtKB:P39831};
DE AltName: Full=Malonic semialdehyde reductase {ECO:0000250|UniProtKB:P39831};
DE EC=1.1.1.298 {ECO:0000250|UniProtKB:P39831};
GN Name=ydfG {ECO:0000250|UniProtKB:P39831}; OrderedLocusNames=STM1511;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
RX PubMed=1537804; DOI=10.1128/jb.174.5.1626-1630.1992;
RA Miller C.G., Hamilton S.;
RT "Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene
RT encoding dipeptidyl carboxypeptidase.";
RL J. Bacteriol. 174:1626-1630(1992).
RN [3]
RP IDENTIFICATION.
RX PubMed=7920643; DOI=10.1038/ng0694-205;
RA Robison K., Gilbert W., Church G.M.;
RT "Large scale bacterial gene discovery by similarity search.";
RL Nat. Genet. 7:205-214(1994).
CC -!- FUNCTION: NADP-dependent dehydrogenase with broad substrate specificity
CC acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-
CC allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously
CC decarboxylated into aminoacetone. Also acts on D-threonine, L-serine,
CC D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate
CC and L-glycerate. Able to catalyze the reduction of the malonic
CC semialdehyde to 3-hydroxypropionic acid. YdfG is apparently
CC supplementing RutE, the presumed malonic semialdehyde reductase
CC involved in pyrimidine degradation since both are able to detoxify
CC malonic semialdehyde. {ECO:0000250|UniProtKB:P39831}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + H(+) +
CC NADPH; Xref=Rhea:RHEA:26438, ChEBI:CHEBI:15378, ChEBI:CHEBI:16510,
CC ChEBI:CHEBI:33190, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.298; Evidence={ECO:0000250|UniProtKB:P39831};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH;
CC Xref=Rhea:RHEA:43524, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58320, ChEBI:CHEBI:58349, ChEBI:CHEBI:58585;
CC EC=1.1.1.381; Evidence={ECO:0000250|UniProtKB:P39831};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P39831}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AE006468; AAL20430.1; -; Genomic_DNA.
DR EMBL; M84575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_460471.1; NC_003197.2.
DR RefSeq; WP_000636564.1; NC_003197.2.
DR AlphaFoldDB; P69936; -.
DR SMR; P69936; -.
DR STRING; 99287.STM1511; -.
DR PaxDb; P69936; -.
DR EnsemblBacteria; AAL20430; AAL20430; STM1511.
DR GeneID; 1253029; -.
DR KEGG; stm:STM1511; -.
DR PATRIC; fig|99287.12.peg.1598; -.
DR HOGENOM; CLU_010194_2_10_6; -.
DR PhylomeDB; P69936; -.
DR BioCyc; SENT99287:STM1511-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0035527; F:3-hydroxypropionate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..248
FT /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG"
FT /id="PRO_0000054829"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 7..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 32..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 54..55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT BINDING 177..185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q05016"
FT CONFLICT 56..70
FT /note="RNRAAIEEMMASLPA -> QPRGHRRDDGLSAS (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27043 MW; A99FEC9188EFC8E4 CRC64;
MIVLVTGATA GFGECIARRF VENGHKVIAT GRRHERLQAL KDELGENVLT AQLDVRNRAA
IEEMMASLPA QWRDIDVLVN NAGLALGLEP AHKASVEDWE TMIDTNNKGL IYMTRAVLPG
MVERNRGHII NIGSTAGSWP YAGGNVYGAT KAFVRQFSLN LRTDLHGTAV RVTDIEPGLV
GGTEFSSVRF KGDDEKAGKT YENTTALTPE DITEAVWWVA TLPAHVNINT VEMMPVTQSF
AGLSVHRS
