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Database: UniProt
Entry: E6VH82_RHOPX
LinkDB: E6VH82_RHOPX
Original site: E6VH82_RHOPX 
ID   E6VH82_RHOPX            Unreviewed;       327 AA.
AC   E6VH82;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   OrderedLocusNames=Rpdx1_0211 {ECO:0000313|EMBL:ADU41854.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU41854.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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DR   EMBL; CP002418; ADU41854.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VH82; -.
DR   STRING; 652103.Rpdx1_0211; -.
DR   KEGG; rpx:Rpdx1_0211; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_7_5; -.
DR   OrthoDB; 9806940at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS01060-MONOMER; -.
DR   Proteomes; UP000001402; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08298; CAD2; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR014187; ADH_Zn_typ-2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR02822; adh_fam_2; 1.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR   Pfam; PF08240; ADH_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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          10..325
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   327 AA;  34541 MW;  EE64C758284E3D18 CRC64;
     MDAMVLTAPG TPLQWQQRDT PHPGDGEVLV TVSACGVCRT DLHVVDGELP NIRYPIIPGH
     EIVGRVAAIG GGVTTHRIGD RVGIPWLGHT CGVCRYCRSG MENLCDAPLF TGYTRDGGFA
     SHAIADARYA FPLGEADDDV AIAPLLCAGL IGWRSLVIAG PAERLGIYGF GAAGHIVAQV
     ARWQGRQVYA FTRGGDVAAQ EFARSLGAVW AGASEELPPE PLDAAIIYAP VGSLVPAALK
     AVRKGGRVVC AGIHMSDIPS FPYDLLWEER QLVSVANLTR QDGIDFLAVA ARAGIRTETH
     AFPLREANAV LTKLRAGELL GAAVLVP
//
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