ID   A0A0G3AHC5_9ACTN        Unreviewed;       334 AA.
AC   A0A0G3AHC5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   29-MAY-2024, entry version 24.
DE   RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase {ECO:0000256|ARBA:ARBA00039387};
DE            EC=1.1.1.329 {ECO:0000256|ARBA:ARBA00039102};
GN   ORFNames=ABB07_26290 {ECO:0000313|EMBL:AKJ13411.1};
OS   Streptomyces incarnatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ13411.1, ECO:0000313|Proteomes:UP000035366};
RN   [1] {ECO:0000313|EMBL:AKJ13411.1, ECO:0000313|Proteomes:UP000035366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX   PubMed=26159526;
RA   Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA   Tamura T.;
RT   "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT   the Nucleoside Antibiotic Sinefungin.";
RL   Genome Announc. 3:e00715-e00715(2015).
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         ECO:0000256|RuleBase:RU361277};
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}.
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DR   EMBL; CP011497; AKJ13411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3AHC5; -.
DR   STRING; 665007.ABB07_26290; -.
DR   PATRIC; fig|665007.5.peg.5583; -.
DR   Proteomes; UP000035366; Chromosome.
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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; 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.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          11..332
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   334 AA;  34575 MW;  27497F633B2E927A CRC64;
     MSTAVVVEAP GRHRLVAHTP REPGPGEALV AVHAVGICGS DREVYQGNRP EGYVRYPLTP
     GHEWSGTVSE VGAGVPAGLV GRKVVGEGFR NCQVCDRCHA GETTLCTDGY EETGFTQPGA
     MAGTLTLPAR LLHVLPDDAD LTAAALLEPA ACVAAAALKA RALPGERVAV VGTGTLGMFA
     VQFLKAVSPA ELLVVGTGND REALARRFGA TGFRLKDQEL PDDMDVVIET AGSASAARTA
     AALLRRGGRL VLTGIPAPGA DGLDPTDLVV RQLEVHTVFG APPDAWAHTV RVFGAGLLDP
     LPLVTHELPL TGFPQAIELV GAGDPKVGKV LLRP
//