ID A0A170RZR0_STRLU Unreviewed; 337 AA.
AC A0A170RZR0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase {ECO:0000256|ARBA:ARBA00039387};
DE EC=1.1.1.329 {ECO:0000256|ARBA:ARBA00039102};
GN ORFNames=SLA_0443 {ECO:0000313|EMBL:BAU81398.1};
OS Streptomyces laurentii.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU81398.1, ECO:0000313|Proteomes:UP000217676};
RN [1] {ECO:0000313|EMBL:BAU81398.1, ECO:0000313|Proteomes:UP000217676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU81398.1,
RC ECO:0000313|Proteomes:UP000217676};
RA Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT ATCC 31255.";
RL Genome Announc. 4:e00360-16(2016).
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; AP017424; BAU81398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A170RZR0; -.
DR KEGG; slau:SLA_0443; -.
DR Proteomes; UP000217676; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08254; hydroxyacyl_CoA_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic 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 Reference proteome {ECO:0000313|Proteomes:UP000217676};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..335
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 337 AA; 35187 MW; E9E75CEF7E27693E CRC64;
MEQMLAARLH VPSRTLRIEE VAKPAPGPGQ VLVKVEAAGV CLSDVHLIDG TLTPLLLRED
TVTLGHEVSG TIAETGPGVT RWTPGQRVVL YAGEVRGGVT YTRGVDYDGG WAEYALSSEH
ALTELPDSIP FDQGAIIPDA VSTPWGAITV TGAVKPAEAV GVWGVGGLGV HAVQLLRAIG
ACPVIAVDPN PTARERALAQ GADLALDPAD PALRERIGAA TRGAGLAAAF DFAGVPAVRE
QALTVLAPKG RLVLAGLTDK PLTVTDGTRF SYLQQQILGH YGSDMPVALP QLLSLLQGGR
LDFSASISGE LPLEKAAEAV ERLENKTGDP IRLILRP
//
