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Database: UniProt
Entry: A0A366IL12_9MICO
LinkDB: A0A366IL12_9MICO
Original site: A0A366IL12_9MICO 
ID   A0A366IL12_9MICO        Unreviewed;       370 AA.
AC   A0A366IL12;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:RBP73123.1};
GN   ORFNames=DFO65_103421 {ECO:0000313|EMBL:RBP73123.1};
OS   Brevibacterium celere.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=225845 {ECO:0000313|EMBL:RBP73123.1, ECO:0000313|Proteomes:UP000253509};
RN   [1] {ECO:0000313|EMBL:RBP73123.1, ECO:0000313|Proteomes:UP000253509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3b_TX {ECO:0000313|EMBL:RBP73123.1,
RC   ECO:0000313|Proteomes:UP000253509};
RA   Lamendella R.;
RT   "Freshwater and sediment microbial communities from various areas in North
RT   America, analyzing microbe dynamics in response to fracking.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RBP73123.1}.
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DR   EMBL; QNSB01000003; RBP73123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366IL12; -.
DR   Proteomes; UP000253509; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000253509};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          19..362
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   370 AA;  38092 MW;  289D20D32C92F36E CRC64;
     MRITGAVLRE MGRERPYAGS RPLAIEELEL DEPGPGEVLI RLTAAGVCHS DLSVVDGNRP
     RPLPMLLGHE GAGIVETLGP GVDDLSVGQS VVTVFLPRCG ECANCRTDGK LPCTPGSATN
     AAGTLPFDGH EVRLHDASGT EVLHHLGASV FATHAVVNRA SLVPIGADVP APIAAVLGCA
     VLTGGGAVLN AGAPRAQDEV MIVGLGGVGM AALLTALSIE TAGVIGVDAN PDKLERAREL
     GATEVFTPDQ LGDRKAAVVV ECAGHPRAFE TAFTATAVGG TTVTVGLPAP DAVSRITPVT
     LTAEARTVIG SYLGSAVSSR DIPVYAQLWR EGKLPVEELI SDTIGLHEIN AAFDALAEGT
     VVRQIIDFRR
//
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