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
//