GenomeNet

Database: UniProt
Entry: U1YDV7_9BURK
LinkDB: U1YDV7_9BURK
Original site: U1YDV7_9BURK 
ID   U1YDV7_9BURK            Unreviewed;       369 AA.
AC   U1YDV7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00021865, ECO:0000256|RuleBase:RU362016};
DE            EC=1.1.1.284 {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
GN   ORFNames=N879_07420 {ECO:0000313|EMBL:ERI33660.1};
OS   Alcaligenes sp. EGD-AK7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERI33660.1, ECO:0000313|Proteomes:UP000016497};
RN   [1] {ECO:0000313|EMBL:ERI33660.1, ECO:0000313|Proteomes:UP000016497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERI33660.1};
RX   PubMed=24407646;
RA   Sagarkar S., Bhardwaj P., Yadav T.C., Qureshi A., Khardenavis A.,
RA   Purohit H.J., Kapley A.;
RT   "Draft genome sequence of atrazine-utilizing bacteria isolated from Indian
RT   agricultural soil.";
RL   Genome Announc. 2:e01149-13(2014).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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}.
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:ERI33660.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AVOG02000012; ERI33660.1; -; Genomic_DNA.
DR   RefSeq; WP_011871467.1; NZ_AVOG02000012.1.
DR   AlphaFoldDB; U1YDV7; -.
DR   GeneID; 84792062; -.
DR   PATRIC; fig|1386079.3.peg.1423; -.
DR   OrthoDB; 9770544at2; -.
DR   Proteomes; UP000016497; Unassembled WGS sequence.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:RHEA.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016497};
KW   Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          10..367
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   369 AA;  39054 MW;  36EFBE2EF10E75C6 CRC64;
     MKSRAAVAFG PGKPLEIVEI DVEPPRKGEV LIKITNTGVC HTDAFTLSGD DPEGLFPVVL
     GHEGAGIVVE VGEGVTSVKP GDHVIPLYTA ECGECLFCKS GKTNLCVAVR ATQGKGLMPD
     GTTRFSYNGQ PLYHYMGCST FSEYTVVAEV SLAKINPDAN PEHVCLLGCG VTTGIGAVHN
     TAKVQPGDSV AIFGLGGIGL AAIQGARQAK AGRIIAIDTN PAKFELARTF GATECLNPKD
     FDKPIHEVLI EMTGWGVDHT FECIGNVNVM RSALEAAHRG WGQSIVIGVA GAGKEISTRP
     FQLVTGRTWK GSAFGGVKGR TQLPGMVEDA MKGEIDLAPF VTHTMGLDEI NHAFDLMHEG
     KSIRTVIHY
//
DBGET integrated database retrieval system