ID A0A0A8WLW4_9SPHN Unreviewed; 339 AA.
AC A0A0A8WLW4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=MBENS4_4653 {ECO:0000313|EMBL:GAM07657.1};
OS Novosphingobium sp. MBES04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM07657.1};
RN [1] {ECO:0000313|EMBL:GAM07657.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBES04 {ECO:0000313|EMBL:GAM07657.1};
RA Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A.,
RA Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.;
RT "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated from
RT Sunken Wood from Suruga Bay, Japan.";
RL Genome Announc. 3:e01373-14(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; DF850491; GAM07657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8WLW4; -.
DR STRING; 1206458.MBENS4_4653; -.
DR HOGENOM; CLU_026673_20_1_5; -.
DR Proteomes; UP000053513; 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; cd08297; CAD3; 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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 Pfam; PF00107; ADH_zinc_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 Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..334
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 339 AA; 35670 MW; DCA9D4B3F431544F CRC64;
MKAAVVREFG KPLVIEEVQV PRPGPGQILV KIAATGVCHT DLHAAEGDWP VKPNPPFIPG
HEGAGHVVAV GQGVTHVKEG DRVGVPWLYS ACGHCTHCLG GWETLCHEQQ NTGYSVNGSF
AEYVLADANY VGRLPDNVSF IDISPILCAG VTVYKGLKVT DTKPGDWVAI SGIGGLGHMA
VQYAKAMGFN VVAVDIDDAK LKLAQDLGAS LTVNARDVDP VAFITKEIGG AQGVLVTAVS
PTAFQQAMGM ARRGGTISLN GLPPGDFPIS IFDTVLNGIT VRGSIVGTRL DLQESLDFAA
QGKVKATVTT DSLENINDVF ARMHKGEIEG RVVLDLENA
//
