ID A0A086H1U6_STRSC Unreviewed; 367 AA.
AC A0A086H1U6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase {ECO:0000256|ARBA:ARBA00039387};
DE EC=1.1.1.329 {ECO:0000256|ARBA:ARBA00039102};
GN ORFNames=IQ62_05560 {ECO:0000313|EMBL:KFG01614.1};
OS Streptomyces scabiei.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1930 {ECO:0000313|EMBL:KFG01614.1, ECO:0000313|Proteomes:UP000028722};
RN [1] {ECO:0000313|EMBL:KFG01614.1, ECO:0000313|Proteomes:UP000028722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4086 {ECO:0000313|EMBL:KFG01614.1,
RC ECO:0000313|Proteomes:UP000028722};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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 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}.
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:KFG01614.1}.
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DR EMBL; JPPX01000047; KFG01614.1; -; Genomic_DNA.
DR RefSeq; WP_037690616.1; NZ_KL997399.1.
DR AlphaFoldDB; A0A086H1U6; -.
DR OrthoDB; 3567264at2; -.
DR Proteomes; UP000028722; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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: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.
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 12..355
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 367 AA; 39408 MW; B5E174158FEB7E99 CRC64;
MATMLALRAH QGAEALALDE MPVPEPGPLD VVVKVASAGL APGIMRLLRM GALKHLPTTL
GHEAAGVVSA IGRDVTGHAV GDRVRVHPLL NCRECDYCRT DRDMMCDQQA MLGHAAFGDA
RMPMYEQYHD GGLAEYIRVP HWLIDSLPDS VSFDVAAKVQ DLANAVRALK CADLPERATL
VVTAATGTMG TATVKLAEHF GVARLILVGR DAERLHRVAG LAGGIPAGVV ALDELPENWS
TDGTLTRRLR ELAPEGADAV IDFIPEGPAL SQTMAGMATG GTLVHMGGNS TPLPLPPIAL
MMHCWRFVTT RACTRQDTTD VLRLLETGTL TVDELITHRF PLTEAIKAMD AIEQRADDPM
WMTVINP
//
