ID G8S739_ACTS5 Unreviewed; 343 AA.
AC G8S739;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AEV85068.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:AEV85068.1};
GN Name=adh {ECO:0000313|EMBL:AEV85068.1};
GN OrderedLocusNames=ACPL_4173 {ECO:0000313|EMBL:AEV85068.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV85068.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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; CP003170; AEV85068.1; -; Genomic_DNA.
DR RefSeq; WP_014691140.1; NZ_LT827010.1.
DR AlphaFoldDB; G8S739; -.
DR STRING; 134676.ACPL_4173; -.
DR KEGG; ase:ACPL_4173; -.
DR PATRIC; fig|134676.3.peg.4089; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_11; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEV85068.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 25..133
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 172..296
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 343 AA; 35924 MW; 8D04519A4FB7F3F5 CRC64;
MKALIFQGPM RMVVEDVPEP VAAAGELLLR VDAVGICGSD VHGYAGETGR RTAGMVMGHE
ISATVLELGD GVTGWSSGDC VAVNPVIGCR QCIRCHAGNT NLCPYRRVIG VDSHYRGGYA
EQIVVPAANA VPLEAGLWQG ALIEPLAVGL QAVRQAGVCR DTEVAVLGAG MIGLAATWAA
WRDGARDVFT GDLDATKVRR AERLGAVGLS LSATTLREAL EARGVTEIAR VVDAIGISAT
IDSALDMVTP GGTVCIVGMG SPQVQLPAYA LTTAERRIVG SFCYSEAHFR EAAEALLDGT
VPVDLFIDRE IGLDEAPEAF RQLASGERAT VKTVIRPTGR QAC
//
