ID G5LPR3_SALET Unreviewed; 358 AA.
AC G5LPR3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Alcohol dehydrogenase class 3 {ECO:0000313|EMBL:EHC38401.1};
GN ORFNames=LTSEALA_2738 {ECO:0000313|EMBL:EHC38401.1};
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:EHC38401.1, ECO:0000313|Proteomes:UP000004642};
RN [1] {ECO:0000313|EMBL:EHC38401.1, ECO:0000313|Proteomes:UP000004642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC38401.1,
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:EHC38401.1}.
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DR EMBL; AFCJ01001171; EHC38401.1; -; Genomic_DNA.
DR AlphaFoldDB; G5LPR3; -.
DR PATRIC; fig|913241.3.peg.2062; -.
DR Proteomes; UP000004642; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08258; Zn_ADH4; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 9..352
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 358 AA; 38902 MW; C7BECE93C3ACC69E CRC64;
MKALARFGKA FGGYKMIDVP EPVCGPEDVI IEIKAAAICG ADMKHYNVDS GSDEFNSVRG
HEFAGRIARV GEKVKDWKVG QRVVSDNSGH VCGVCPACEQ GDFLCCTEKV NLGLDNNTWG
GGFSKYCLVP GEILKIHRHA LWEIPEGVDY EEAAVLDPIC NAYKSIAQQS KFLPGQDVVV
IGTGPLGLFS VQMARIMGAV NIVVVGLDED VPVRFPVAKE LGATAFVNGS TEDVVARCRE
ICGKDNLGLV IECSGANIAL KQAIDMLRPN GEVVRVGMGF KPLDFSINDI TSWNKSIIGH
MAYDSTSWRN AIRLLASGAI KVKPMITHRI GLSQWREGFD AMVDKTAIKV IMTYDFDE
//
