YDFG_SHIFL
ID YDFG_SHIFL Reviewed; 248 AA.
AC Q83RE8; Q7UCH2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=SF1556, S1681;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43145.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17037.1; -; Genomic_DNA.
DR RefSeq; NP_707438.2; NC_004337.2.
DR AlphaFoldDB; Q83RE8; -.
DR SMR; Q83RE8; -.
DR STRING; 198214.SF1556; -.
DR EnsemblBacteria; AAN43145; AAN43145; SF1556.
DR EnsemblBacteria; AAP17037; AAP17037; S1681.
DR GeneID; 1024772; -.
DR KEGG; sfl:SF1556; -.
DR KEGG; sfx:S1681; -.
DR PATRIC; fig|198214.7.peg.1838; -.
DR HOGENOM; CLU_010194_2_10_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0035527; F:3-hydroxypropionate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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_0000054830"
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"
SQ SEQUENCE 248 AA; 27236 MW; 8CBC8781B879418F CRC64;
MIVLVTGATA GFGECITRRF IQQGHKVIAT GRRQERLQEL TDELGDNLYI AQLDVRNRAA
IEEMLASLPA EWSNIDILVN NAGLALGMEP AHKASVEDWE TMIDTNNKGL VYMTRAVLPG
MVERNHGHII NIGSTAGSWP YAGGNVYGAT KAFVRQFSLN LRTDLHGTTV RVTDIEPGLV
GGTEFSNVRF KGDDGKAEKT YQNTVALTPE DVSEAVWWVS TLPAHVNINT LEMMPVTQSY
AGLNVHRQ
