ID G5LP35_SALET Unreviewed; 248 AA.
AC G5LP35;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=NADP-dependent 3-hydroxy acid dehydrogenase YdfG {ECO:0000256|ARBA:ARBA00044065};
DE EC=1.1.1.298 {ECO:0000256|ARBA:ARBA00044050};
DE EC=1.1.1.381 {ECO:0000256|ARBA:ARBA00044059};
DE AltName: Full=L-allo-threonine dehydrogenase {ECO:0000256|ARBA:ARBA00044349};
DE AltName: Full=Malonic semialdehyde reductase {ECO:0000256|ARBA:ARBA00044271};
GN ORFNames=LTSEALA_2461 {ECO:0000313|EMBL:EHC39213.1};
OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC39213.1, ECO:0000313|Proteomes:UP000004642};
RN [1] {ECO:0000313|EMBL:EHC39213.1, ECO:0000313|Proteomes:UP000004642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC39213.1,
RC ECO:0000313|Proteomes:UP000004642};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:0000256|ARBA:ARBA00043756};
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:0000256|ARBA:ARBA00043812};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC39213.1}.
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DR EMBL; AFCJ01001064; EHC39213.1; -; Genomic_DNA.
DR AlphaFoldDB; G5LP35; -.
DR SMR; G5LP35; -.
DR PATRIC; fig|913241.3.peg.1862; -.
DR Proteomes; UP000004642; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05346; SDR_c5; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43086:SF3; NADP-DEPENDENT 3-HYDROXY ACID DEHYDROGENASE YDFG; 1.
DR PANTHER; PTHR43086; VERY-LONG-CHAIN 3-OXOOACYL-COA REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
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
//
