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Database: UniProt/TrEMBL
Entry: Q211I5_RHOPB
LinkDB: Q211I5_RHOPB
Original site: Q211I5_RHOPB 
ID   Q211I5_RHOPB            Unreviewed;       341 AA.
AC   Q211I5;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   OrderedLocusNames=RPC_3411 {ECO:0000313|EMBL:ABD88951.1};
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD88951.1};
RN   [1] {ECO:0000313|EMBL:ABD88951.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18 {ECO:0000313|EMBL:ABD88951.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) 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; CP000301; ABD88951.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q211I5; -.
DR   STRING; 316056.RPC_3411; -.
DR   KEGG; rpc:RPC_3411; -.
DR   eggNOG; COG1064; Bacteria.
DR   HOGENOM; CLU_026673_20_7_5; -.
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          24..339
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   341 AA;  36498 MW;  15D87F4694F9B6F3 CRC64;
     MYPWLSRIDG AEWQMQAMVL TAPGAPLLMQ QRATPQPGDG EVRVKVNACG VCRTDLHVVD
     GELPNIRYPI IPGHEIVGRV EAVGRGVSTH QVGDRVGIPW LGHTCRVCRY CRAGQENLCD
     APLFTGYTRD GGFASHTIAD ARYAFALGEL GDDVAIAPLL CAGLIGWRAL VIAGQAERLG
     LYGFGAAAHI VAQLARWQGR RVYAFTRHGD AAAQNFARSL GVEWAGGSDE LPGEPLDAAI
     IFAPAGELVP AALRAVRKGG RVVCAGIHMS DIPSFPYSLL WEERQLVSVA NLTRQDGVDF
     LKVAQQAGIK TETHAYPLPE ANAVLDRLRA GDVLGAAVLV P
//
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