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Database: UniProt
Entry: E8AY78_SALMO
LinkDB: E8AY78_SALMO
Original site: E8AY78_SALMO 
ID   E8AY78_SALMO            Unreviewed;       372 AA.
AC   E8AY78;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00021865, ECO:0000256|RuleBase:RU362016};
DE            EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016};
OS   Salmonella enterica subsp. enterica serovar Montevideo str. 609458-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=858317 {ECO:0000313|EMBL:AEK68097.1};
RN   [1] {ECO:0000313|EMBL:AEK68097.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=609458-1 {ECO:0000313|EMBL:AEK68097.1};
RX   PubMed=21345093; DOI=10.1056/NEJMc1100443;
RA   Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E.,
RA   Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J.,
RA   Stones R.;
RT   "Identification of a salmonellosis outbreak by means of molecular
RT   sequencing.";
RL   N. Engl. J. Med. 364:981-982(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001030,
CC         ECO:0000256|RuleBase:RU362016};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001646};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001146};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000781};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU362016};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000256|ARBA:ARBA00010902,
CC       ECO:0000256|RuleBase:RU362016}.
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DR   EMBL; JF711521; AEK68097.1; -; Genomic_DNA.
DR   RefSeq; WP_000842142.1; NZ_AETF01000033.1.
DR   AlphaFoldDB; E8AY78; -.
DR   PATRIC; fig|858317.4.peg.1578; -.
DR   GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR   GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   CDD; cd08300; alcohol_DH_class_III; 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; IPR014183; ADH_3.
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   NCBIfam; TIGR02818; adh_III_F_hyde; 1.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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|RuleBase:RU362016};
KW   NAD {ECO:0000256|RuleBase:RU362016};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362016}; Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          12..367
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   372 AA;  39285 MW;  45F0F5986B65FD1F CRC64;
     MKSRAAVAFG PGQPLKIVEI DVAPPKKGEV LVKITHTGVC HTDAFTLSGD DPEGVFPAVL
     GHEGGGVVVE VGEGVTSLKP GDHVIPLYTA ECGECKFCKS GKTNLCQAVR ATQGKGLMPD
     GTTRFSYNGE PVYHYMGTST FSEYTVCAEI SLAKVNPQAP LDKVCLLGCG VTTGIGAVHN
     TAKVKAGDTV AVFGLGGIGL AVIQGAVQAK AGRILAVDTN PEKFTLAGEM GATDFINPND
     YDKPIQDVIV ELTDGGVDFS FECIGNVNVM RAALECCHKG WGESIIIGVA GAGQEIKTRP
     FQLVTGRVWR GSAFGGVKGR TQLPGMVEDA MNGKIRLDPF ITHRLPLEQI NDAFELMHQG
     KSIRTVIHFS DN
//
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