ID A0A0J7ZGL0_STRVR Unreviewed; 368 AA.
AC A0A0J7ZGL0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:KMS75211.1};
GN ORFNames=ACM01_11265 {ECO:0000313|EMBL:KMS75211.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS75211.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS75211.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS75211.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-2015) 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:KMS75211.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFNT01000009; KMS75211.1; -; Genomic_DNA.
DR RefSeq; WP_048581000.1; NZ_LGUR01000249.1.
DR AlphaFoldDB; A0A0J7ZGL0; -.
DR PATRIC; fig|1938.3.peg.2249; -.
DR OrthoDB; 334894at2; -.
DR Proteomes; UP000037432; 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; cd08278; benzyl_alcohol_DH; 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; 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 13..364
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 368 AA; 37994 MW; 17C55B9E82D297BA CRC64;
MRIQAAVFEK QDGPFQLQDV ELDDPEAGEV VVRIAATGIC HTDGLARHGD LPFPAPGVLG
HEGAGVVTAV GPGVTSVREG DHVVIGWPWC GECRNCLAGE PRYCARLGEL LVSGVRPGTG
ASALRRPDGG VLHGHFFGQS SFATHSLTRA NSLVKVPHDV PLDLLGPLAC GLSTGAGAVL
NTLRPQTGSS LVIYGTGSVG LAAVMAARNS GSTTIIAVDR HTSRLELAAE LGATHTVNAA
DTDPVAAVHD ICGGPADNAL ECTGIISVVR QAADSVGMLG TCALIGGAPA GAEFTLDHLT
TLWGKRIVGV LGGGGRSTQL IGALIELYRQ GRFPMERLVS WFAFDRIEQA LAASYAGDVI
KPIVRMPA
//