ID A0A101V5A2_9ACTN Unreviewed; 329 AA.
AC A0A101V5A2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase {ECO:0000256|ARBA:ARBA00039387};
DE EC=1.1.1.329 {ECO:0000256|ARBA:ARBA00039102};
GN ORFNames=AQJ91_02515 {ECO:0000313|EMBL:KUO22694.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO22694.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO22694.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO22694.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA)
CC with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose
CC (amino-DOI). {ECO:0000256|ARBA:ARBA00037678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-scyllo-inosamine + NAD(+) = 3-amino-2,3-dideoxy-
CC scyllo-inosose + H(+) + NADH; Xref=Rhea:RHEA:33883,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65002, ChEBI:CHEBI:65003; EC=1.1.1.329;
CC Evidence={ECO:0000256|ARBA:ARBA00036792};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-scyllo-inosamine + NADP(+) = 3-amino-2,3-dideoxy-
CC scyllo-inosose + H(+) + NADPH; Xref=Rhea:RHEA:33879,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65002, ChEBI:CHEBI:65003; EC=1.1.1.329;
CC Evidence={ECO:0000256|ARBA:ARBA00036830};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00037908}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. DOIA dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00038004}.
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:KUO22694.1}.
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DR EMBL; LMXB01000011; KUO22694.1; -; Genomic_DNA.
DR RefSeq; WP_067015534.1; NZ_KQ949075.1.
DR AlphaFoldDB; A0A101V5A2; -.
DR STRING; 909626.AQJ91_02515; -.
DR OrthoDB; 9797931at2; -.
DR Proteomes; UP000053260; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08234; threonine_DH_like; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053260}.
FT DOMAIN 4..327
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 329 AA; 34803 MW; F91D8DDE3DF1D83E CRC64;
MKAAVIESVG RAVVSEVPDP TPGPREVVVE VAACGICGTD LHILQGEFAP KLPIVPGHEF
AGAVVGVGTQ VTELTVGDRV AVDPSLYCYE CRNCRTGHNN LCERWAAIGV TTAGGAAQYA
VAPVANCAKL PEHVRTQDAA LVEPLSCAVR GYDVLKSRLG AHVLIYGSGT MGLMMLELAK
RTGAASVDIV DVNPTRLETA RRLGVSASAA HADELDRPQG WDLVVDATGN AAAIQDGLDR
VAKAGTFLQF GVADYATRVT IDPYRIYNQE ITITGSMAVL HSFERAAELF ANGVLDPEIF
ISDRIPLDQY PQALEQFAAG VGRKIVVVP
//
