SPNN_SACSN
ID SPNN_SACSN Reviewed; 332 AA.
AC Q9ALN5;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase {ECO:0000303|PubMed:18345667};
DE EC=1.1.1.384 {ECO:0000269|PubMed:18345667};
DE AltName: Full=dTDP-3,4-diketo-2,6-dideoxy-D-glucose 3-ketoreductase {ECO:0000303|PubMed:18345667};
GN Name=spnN {ECO:0000303|PubMed:11358695};
OS Saccharopolyspora spinosa.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=60894;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11358695; DOI=10.1016/s1074-5521(01)00029-1;
RA Waldron C., Matsushima P., Rosteck P.R. Jr., Broughton M.C., Turner J.,
RA Madduri K., Crawford K.P., Merlo D.J., Baltz R.H.;
RT "Cloning and analysis of the spinosad biosynthetic gene cluster of
RT Saccharopolyspora spinosa.";
RL Chem. Biol. 8:487-499(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=NRRL 18537;
RX PubMed=18345667; DOI=10.1021/ja0771383;
RA Hong L., Zhao Z., Melancon C.E. III, Zhang H., Liu H.W.;
RT "In vitro characterization of the enzymes involved in TDP-D-forosamine
RT biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa.";
RL J. Am. Chem. Soc. 130:4954-4967(2008).
CC -!- FUNCTION: Involved in the biosynthesis of forosamine ((4-
CC dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly
CC deoxygenated sugar component of several bioactive natural products such
CC as the insecticidal spinosyns A and D (PubMed:11358695,
CC PubMed:18345667). Catalyzes the reduction of the C-3 keto moiety of
CC dTDP-3,4-diketo-2,6-dideoxy-alpha-D-glucose to yield dTDP-4-keto-2,6-
CC dideoxy-alpha-D-glucose (PubMed:18345667). NADPH is the better
CC reductant, however NADH can also be used (PubMed:18345667).
CC {ECO:0000269|PubMed:11358695, ECO:0000269|PubMed:18345667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-
CC 3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH;
CC Xref=Rhea:RHEA:44624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84537, ChEBI:CHEBI:84540;
CC EC=1.1.1.384; Evidence={ECO:0000269|PubMed:18345667};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18345667}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate the
CC pseudoaglycone (PSA) containing tri-O-methyl rhamnose, but lacking the
CC dimethylamino sugar forosamine. {ECO:0000269|PubMed:11358695}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AY007564; AAG23275.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ALN5; -.
DR SMR; Q9ALN5; -.
DR STRING; 994479.GL877879_gene4833; -.
DR KEGG; ag:AAG23275; -.
DR BioCyc; MetaCyc:MON-16620; -.
DR BRENDA; 1.1.1.384; 13744.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase.
FT CHAIN 1..332
FT /note="dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-
FT reductase"
FT /id="PRO_0000444243"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 12..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 58
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
SQ SEQUENCE 332 AA; 36133 MW; A3A9F3561461ABCE CRC64;
MRKPVRIGVL GCASFAWRRM LPAMCDVAET EVVAVASRDP AKAERFAARF ECEAVLGYQR
LLERPDIDAV YVPLPPGMHA EWIGKALEAD KHVLAEKPLT TTASDTARLV GLARRKNLLL
RENYLFLHHG RHDVVRDLLQ SGEIGELREF TAVFGIPPLP DTDIRYRTEL GGGALLDIGV
YPARAARHFL LGPLTVLGAS SHEAQESGVD LSGSVLLQSE GGTVAHLGYG FVHHYRSAYE
LWGSRGRIVV DRAFTPPAEW QAVIRIERKG VVDELSLPAE DQVRKAVTAF ARDIRAGTGV
DDPAVAGDSG ESMIQQAALV EAIGQARRCG ST
