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Database: UniProt
Entry: A0A0H2LUW0_VARPD
LinkDB: A0A0H2LUW0_VARPD
Original site: A0A0H2LUW0_VARPD 
ID   A0A0H2LUW0_VARPD        Unreviewed;       336 AA.
AC   A0A0H2LUW0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=VPARA_49220 {ECO:0000313|EMBL:KLN53984.1};
OS   Variovorax paradoxus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN53984.1, ECO:0000313|Proteomes:UP000035170};
RN   [1] {ECO:0000313|EMBL:KLN53984.1, ECO:0000313|Proteomes:UP000035170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBEA6 {ECO:0000313|EMBL:KLN53984.1,
RC   ECO:0000313|Proteomes:UP000035170};
RA   Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA   Daniel R.;
RT   "Genome sequence of Variovorax paradoxus TBEA6.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:KLN53984.1}.
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DR   EMBL; JZWI01000028; KLN53984.1; -; Genomic_DNA.
DR   RefSeq; WP_047786389.1; NZ_JZWI01000028.1.
DR   AlphaFoldDB; A0A0H2LUW0; -.
DR   PATRIC; fig|34073.19.peg.5038; -.
DR   Proteomes; UP000035170; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; 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   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 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:UP000035170};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          13..333
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   336 AA;  35294 MW;  F505B106C9DB49FD CRC64;
     MKAIGYYQPL PIDNPESLQD IELPAPVAGP RDLLVRVKAI SVNPVDTKVR KNMAPEAGQA
     KVLGWDAAGT VEAIGAGVKN FKVGDRVYYA GSIVRPGANA ELHAVDERIV ALAPRSLDDA
     QAAALPLTTI TAYELLFDRL QVPKNGGAGQ TLLVTGGAGG VGSILIQLAR QLTQLRVVAT
     ASRAETRAWC LALGAHAVID HSKPLAAELK AAGIGEVDMV ASLTQTGQHY AQIIESLKPQ
     GQLAVIDDLP ALDAMPLKTK CISLHWEMMF ARSRFETPDI AEQGALLAEV AALVDAGRIR
     TTANASFGAI NAANLRKAHA LIESGKAQGK VVLAGF
//
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