SPNO_SACSN
ID SPNO_SACSN Reviewed; 486 AA.
AC Q9ALN6;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase {ECO:0000303|PubMed:18345667};
DE EC=4.2.1.159 {ECO:0000269|PubMed:18345667};
DE AltName: Full=2,3-dehydratase {ECO:0000303|PubMed:18345667};
DE AltName: Full=dTDP-4-keto-6-deoxy-D-glucose 2,3-dehydratase {ECO:0000303|PubMed:18345667};
GN Name=spnO {ECO:0000303|PubMed:11358695};
GN ORFNames=A8926_6443 {ECO:0000312|EMBL:PKW18366.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44228;
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, 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 removal of the hydroxyl group at
CC position C-2 of the hexose ring of dTDP-4-dehydro-6-deoxy-alpha-D-
CC glucopyranose, and the oxidation of the hydroxyl group at position C-3
CC to form a carbonyl functionality (PubMed:18345667). The product of the
CC reaction, dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose, is a highly
CC unstable diketosugar, which spontaneously forms dTDP-3,4-didehydro-2,6-
CC dideoxy-alpha-D-glucose (PubMed:18345667).
CC {ECO:0000269|PubMed:11358695, ECO:0000269|PubMed:18345667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3,4-didehydro-
CC 2,6-dideoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:47972,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57649, ChEBI:CHEBI:84540;
CC EC=4.2.1.159; Evidence={ECO:0000269|PubMed:18345667};
CC -!- SUBUNIT: Homodimer. {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 -!- MISCELLANEOUS: Two binding sites (pockets A and B) for the dTDP-sugar
CC ligands have been identified in each subunit. It seems that pocket A
CC represents the active site and pocket B is a vestige of the gene
CC duplication event. {ECO:0000250|UniProtKB:O52793}.
CC -!- SIMILARITY: Belongs to the hexose 2,3-dehydratase family.
CC {ECO:0000305}.
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DR EMBL; AY007564; AAG23276.1; -; Genomic_DNA.
DR EMBL; PJNB01000001; PKW18366.1; -; Genomic_DNA.
DR RefSeq; WP_010309423.1; NZ_PJNB01000001.1.
DR AlphaFoldDB; Q9ALN6; -.
DR SMR; Q9ALN6; -.
DR STRING; 994479.GL877879_gene4834; -.
DR EnsemblBacteria; PKW18366; PKW18366; A8926_6443.
DR KEGG; ag:AAG23276; -.
DR BioCyc; MetaCyc:MON-16619; -.
DR BRENDA; 4.2.1.159; 13744.
DR Proteomes; UP000233786; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.79.40; -; 2.
DR InterPro; IPR005212; EvaA-like.
DR InterPro; IPR038153; EvaA-like_sf.
DR Pfam; PF03559; Hexose_dehydrat; 2.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..486
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-
FT dehydratase"
FT /id="PRO_0000444211"
FT REGION 149..153
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 1; pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 383..385
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 2; pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 388..389
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 2; pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 421..424
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 1; pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 66
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="1"
FT /note="from pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 187
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="2"
FT /note="from pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 304
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="2"
FT /note="from pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 367
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="2"
FT /note="from pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
SQ SEQUENCE 486 AA; 54393 MW; 218A730C840BA708 CRC64;
MSSSVEAEAS AAAPLGSNNT RRFVDSALSA CNGMIPTTEF HCWLADRLGE NSFETNRIPF
DRLSKWKFDA STENLVHADG RFFTVEGLQV ETNYGAAPSW HQPIINQAEV GILGILVKEI
DGVLHCLMSA KMEPGNVNVL QLSPTVQATR SNYTQAHRGS VPPYVDYFLG RGRGRVLVDV
LQSEQGSWFY RKRNRNMVVE VQEEVPVLPD FCWLTLGQVL ALLRQDNIVN MDTRTVLSCI
PFHDSATGPE LAASEEPFRQ AVARSLSHGI DSSSISEAVG WFEEAKARYR LRATRVPLSR
VDKWYRTDTE IAHQDGKYFA VIAVSVSATN REVASWTQPM IEPREQGEIA LLVKRIGGVL
HGLVHARVEA GYKWTAEIAP TVQCSVANYQ STPSNDWPPF LDDVLTADPE TVRYESILSE
EGGRFYQAQN RYRIIEVHED FAARPPSDFR WMTLGQLGEL LRSTHFLNIQ ARSLVASLHS
LWALGR
