ID A0A1Y5SBR1_9RHOB Unreviewed; 327 AA.
AC A0A1Y5SBR1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=adh {ECO:0000313|EMBL:SLN37130.1};
GN ORFNames=PEL8287_01774 {ECO:0000313|EMBL:SLN37130.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN37130.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN37130.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN37130.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFL01000004; SLN37130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5SBR1; -.
DR OrthoDB; 5295340at2; -.
DR Proteomes; UP000193827; Unassembled WGS sequence.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:SLN37130.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193827}.
FT DOMAIN 9..325
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 327 AA; 35123 MW; E10E5D995BE45C27 CRC64;
MRAMVLREGA SSLVLEQLAP PGCGPRQVRL RVEACGVCRT DLHIVDGDLK KPVFPLIPGH
EIVGRITETG PDVRGLTLGQ RVGVPWLGQT CGQCQYCRMG RENLCDAPGF TGYTLNGGYA
EECVADAAYV FPLPQDVEPA GLAPLLCAGL IGYRSYRMAG DAGRLGFYGF GAAAHILVQI
AAWQGREVYA FTRPGDLAGQ EFARQLGAVW AGGSDQRPDV ALDAAILFAP VGALVPRALK
TLRKGGRVVC AGIHMSDIPS FPYADLWHER QVMSVANLTR QDGDEFFPLA QKADVRTHTT
PYPLEKANEA LDDLRAGRLK GAAVLLP
//