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Database: UniProt
Entry: A0A1V2GVZ5_9PROT
LinkDB: A0A1V2GVZ5_9PROT
Original site: A0A1V2GVZ5_9PROT 
ID   A0A1V2GVZ5_9PROT        Unreviewed;       337 AA.
AC   A0A1V2GVZ5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=BKE38_26290 {ECO:0000313|EMBL:ONG45628.1};
OS   Pseudoroseomonas deserti.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Pseudoroseomonas.
OX   NCBI_TaxID=1817963 {ECO:0000313|EMBL:ONG45628.1, ECO:0000313|Proteomes:UP000188879};
RN   [1] {ECO:0000313|EMBL:ONG45628.1, ECO:0000313|Proteomes:UP000188879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3 {ECO:0000313|EMBL:ONG45628.1,
RC   ECO:0000313|Proteomes:UP000188879};
RA   Subhash Y., Lee S.;
RT   "Draft Genome sequence of Roseomonas sp. strain M3.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC       {ECO:0000256|RuleBase:RU364000}.
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:ONG45628.1}.
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DR   EMBL; MLCO01000344; ONG45628.1; -; Genomic_DNA.
DR   RefSeq; WP_076960228.1; NZ_MLCO01000344.1.
DR   AlphaFoldDB; A0A1V2GVZ5; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000188879; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08252; AL_MDR; 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; IPR014182; ADH_Zn_typ-1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR02817; adh_fam_1; 1.
DR   PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU364000};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188879};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          13..334
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   337 AA;  36135 MW;  708EF0EE08C09FAB CRC64;
     MKAIGYQVPG AITRDDALVD IELPRPEARG RDLLVQVQAV SVNPVDTKIR RNVTPDAGQW
     KLLGWDAVGT VVAMGAGASL FKVGDVVAYA GSLIRPGTNA EFHLVDERIV GRAPKNLSIA
     EAAALPLTAI TAWEALFHRL EVARPVRGAA SAILIIGGAG GVGSIAVQLA RQLTDLTVIA
     TASRPETQDW VRQMGAHQVI DHRQPLAAQV AALGLGAPAF VFSTTETGQH LAEIAELIAP
     QGRFCLIDDP DTLDVNRFKR KSVSIHWELM FTRPIFETAD MDEQGRLLNE VSRLVEAGTL
     RTTLAETFGT INAANLKRAH ALIESGKARG KIVLEGF
//
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