YDFG_ECO57
ID YDFG_ECO57 Reviewed; 248 AA.
AC Q8X505; Q7ADX9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=Z2158, ECs2148;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56223.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35571.1; -; Genomic_DNA.
DR PIR; C85720; C85720.
DR PIR; D90897; D90897.
DR RefSeq; NP_310175.1; NC_002695.1.
DR RefSeq; WP_000636568.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X505; -.
DR SMR; Q8X505; -.
DR STRING; 155864.EDL933_2094; -.
DR EnsemblBacteria; AAG56223; AAG56223; Z2158.
DR EnsemblBacteria; BAB35571; BAB35571; ECs_2148.
DR GeneID; 917355; -.
DR KEGG; ece:Z2158; -.
DR KEGG; ecs:ECs_2148; -.
DR PATRIC; fig|386585.9.peg.2256; -.
DR eggNOG; COG4221; Bacteria.
DR HOGENOM; CLU_010194_2_10_6; -.
DR OMA; WRWMWET; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000054827"
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; 27263 MW; E9350F9A4586F4B3 CRC64;
MIVLVTGATA GFGECITRRF IQQGHKVIAT GRRQERLQEL KDELGDNLYI AQLDVRNRAA
IEEMLASLPA EWCNIDILVN NAGLALGMEP AHKASIEDWE TMIDTNNKGL VYMTRAVLPG
MVERNHGHII NIGSTAGSWP YAGGNVYGAT KAFVRQFSLN LRTDLHGTAV RVTDIEPGLV
GGTEFSNVRF KGDDGKAEKT YQNTVALTPE DVSEAVWWVS TLPAHVNINT LEMMPVTQSY
AGLNVHRQ
