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Database: UniProt
Entry: A0A0P1HGD9_9RHOB
LinkDB: A0A0P1HGD9_9RHOB
Original site: A0A0P1HGD9_9RHOB 
ID   A0A0P1HGD9_9RHOB        Unreviewed;       337 AA.
AC   A0A0P1HGD9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=PH5382_03106 {ECO:0000313|EMBL:CUH89160.1};
OS   Phaeobacter sp. CECT 5382.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH89160.1, ECO:0000313|Proteomes:UP000050782};
RN   [1] {ECO:0000313|EMBL:CUH89160.1, ECO:0000313|Proteomes:UP000050782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH89160.1,
RC   ECO:0000313|Proteomes:UP000050782};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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}.
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DR   EMBL; CYSG01000016; CUH89160.1; -; Genomic_DNA.
DR   RefSeq; WP_058335257.1; NZ_CYSG01000016.1.
DR   AlphaFoldDB; A0A0P1HGD9; -.
DR   STRING; 1712645.PH5382_03106; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000050782; 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:UP000050782};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          10..334
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   337 AA;  36136 MW;  BA219D1BA40A8CA7 CRC64;
     MKAVGYFETG SIERADALVD LNMDRPAPTG RDLLVKVRAV SVNPVDYKIR QSRPPETDQP
     AVLGWDAVGE VVEVGNDTSL FKPGDQVWYA GAINRPGTNA EFHLVDERIV GKAPKSVSDA
     QAAALPLTTL TAYEMLFDRL RVATPVPGAA NAVVIIGGSG GVGSIAIQLL RALTDLTVIA
     TASREETKDW VKTLGAHHVI DHSKPLTPQI ESLGLGAPGF VFSTTHTHQY VEQAAEFIAP
     QGRFGLIDDP ESLNIMPFKV KAVSTHWELM FTRPLFETPD MARQGEILNE AAQLLDAGKI
     SSTATETLGV INADNLKKAH AILESGAARG KLVLEGF
//
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