ID A0A1W9JH09_9PROT Unreviewed; 361 AA.
AC A0A1W9JH09;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OQW71143.1};
GN ORFNames=BVN33_16245 {ECO:0000313|EMBL:OQW71143.1};
OS Proteobacteria bacterium ST_bin13.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978761 {ECO:0000313|EMBL:OQW71143.1, ECO:0000313|Proteomes:UP000192661};
RN [1] {ECO:0000313|EMBL:OQW71143.1, ECO:0000313|Proteomes:UP000192661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin13 {ECO:0000313|EMBL:OQW71143.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:OQW71143.1}.
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DR EMBL; MSXQ01000026; OQW71143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9JH09; -.
DR Proteomes; UP000192661; 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; cd08279; Zn_ADH_class_III; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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; 2.
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..358
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 361 AA; 37824 MW; 40996436A241265B CRC64;
MKAAVLYEPK TALVIEDIQV SKPGPREVLI RTVACGVCRS DLHFIEGSFP HPMPTVPGHE
AAGIVEAVGS DVARLKVGDH VITFFTVFCG SCEMCVTGRP SLCIDPSTRR PKGAEPRIAL
KDGTPLAPFL NLSAFAEMML VHENACVAIS KDMPLDRAAL LGCAVITGAG SIFNDSRLRS
GETVAVIGCG GIGLSAINAA KIAGAGKIIA IDPVADKRAL AERLGATHSF DSNDPDLAKK
VIALTGGGVD YAIEAVGRPA TAELAWALLK RGGTATILGM IAPGNMVSLP GPSFLTGKKL
QGSLLGSTRF PIDMPRLVQL YLDGKLDLDT MVAERITLDG VNDAIDKLRT GDTVRSVIEF
N
//
