ID A0A0D5LWI7_9GAMM Unreviewed; 346 AA.
AC A0A0D5LWI7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alcohol dehydrogenase GroES domain protein {ECO:0000313|EMBL:AJY48604.1};
GN ORFNames=KO116_00092 {ECO:0000313|EMBL:AJY48604.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY48604.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY48604.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY48604.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP011052; AJY48604.1; -; Genomic_DNA.
DR RefSeq; WP_035556215.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5LWI7; -.
DR STRING; 1504981.KO116_00092; -.
DR KEGG; hak:KO116_00092; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_11_2_6; -.
DR OrthoDB; 9785812at2; -.
DR Proteomes; UP000028645; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08260; Zn_ADH6; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic 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; PTHR43401:SF5; ALCOHOL DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 10..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 346 AA; 36784 MW; 96DDAE78A7FE3C3A CRC64;
MKAVVFEQFS APPRIQQLPD PTPEAHGVVV KVMANGVCRS DWHGWVGHDT DIQLPHVPGH
ELSGVVEVVG KDVKKWRIGD RVTVPFVGGC GTCPECHSGN HQVCDSQFQP GFTHWGSFAE
YVSIHYADVN LVALPETLDF ATAASLGCRF VTSFRAVVDQ GKTSAGQWVA VHGCGGVGLS
AVMIANAIGA NVVAIDISEE ALNLARQLGA TATVNAAKVP NVVEAVAEIT RGGAHVSLDA
LGHPTTCFNS ISNLRKRGKH VQVGLMLAEN STPAIPMSKV IANELEILGS HGMQAHRYDA
MLAMIESGKL APEKLIGKRI NLEQSIDALM NMDKFEGAGV TVVTEF
//
