OLEV_STRAT
ID OLEV_STRAT Reviewed; 474 AA.
AC Q9RR31;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase {ECO:0000303|Ref.2};
DE EC=4.2.1.159 {ECO:0000269|Ref.2};
DE AltName: Full=2,3-dehydratase {ECO:0000303|PubMed:10770761};
GN Name=oleV {ECO:0000303|PubMed:10770761};
GN Synonyms=orf10 {ECO:0000303|Ref.2};
OS Streptomyces antibioticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1890;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205
RC {ECO:0000312|EMBL:AAD55451.1};
RX PubMed=10770761; DOI=10.1128/aac.44.5.1266-1275.2000;
RA Aguirrezabalaga I., Olano C., Allende N., Rodriguez L., Brana A.F.,
RA Mendez C., Salas J.A.;
RT "Identification and expression of genes involved in biosynthesis of L-
RT oleandrose and its intermediate L-olivose in the oleandomycin producer
RT Streptomyces antibioticus.";
RL Antimicrob. Agents Chemother. 44:1266-1275(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=Tu99;
RA Draeger G., Park S.-H.H., Floss H.G.;
RT "Mechanism of the 2-deoxygenation step in the biosynthesis of the
RT deoxyhexose moieties of the antibiotics granaticin and oleandomycin.";
RL J. Am. Chem. Soc. 121:2611-2612(1999).
CC -!- FUNCTION: Involved in the biosynthesis of one of the two 2,6-
CC deoxysugars, dTDP-L-oleandrose, attached to the macrolactone ring
CC oleandolide to produce the aglycone antibiotic oleandomycin
CC (PubMed:10770761, Ref.2). Catalyzes the removal of the hydroxyl group
CC at 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 (Ref.2). The product of the reaction,
CC dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose, is a highly unstable
CC diketosugar, which spontaneously forms dTDP-3,4-didehydro-2,6-dideoxy-
CC alpha-D-glucose (Ref.2). {ECO:0000269|PubMed:10770761,
CC ECO:0000269|Ref.2}.
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|Ref.2};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:10770761,
CC ECO:0000305|Ref.2}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O52793}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF055579; AAD55451.1; -; Genomic_DNA.
DR PIR; T51103; T51103.
DR AlphaFoldDB; Q9RR31; -.
DR SMR; Q9RR31; -.
DR KEGG; ag:AAD55451; -.
DR BioCyc; MetaCyc:MON-17064; -.
DR BRENDA; 4.2.1.159; 5974.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; 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 Antibiotic biosynthesis; Lyase.
FT CHAIN 1..474
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-
FT dehydratase"
FT /id="PRO_0000444213"
FT REGION 137..141
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 1; pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 375..377
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 2; pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 380..381
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 2; pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 413..416
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 1; pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 54
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 176
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 296
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 359
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 474 AA; 53064 MW; 3F20BDB717E70CAF CRC64;
MIWGIPAMSE AMGSVPTAGS EVSSTCAFLS WLDARRRANR LTVEHVPFRE LSGWQFDENT
GNLRHTSGRF FSIEGLRVRT DHCWFGSWTQ PIIVQPEIGI LGLLVKRFDG ILHVLVQAKN
EPGNIGGLQL SPTVQATRSN YTRVHRGGGV RYLEYFASPR GRGRVLADVL QSEQGSWFLH
KRNRNMVVEA LDDVPLDDDF HWISLGGLRK LLLRPHLVNM DTRTVLSCLP PDPAPDGRQP
PAPAAPFAAA VTRSLTRGAT ALHTMGEILG WLTDERSRRE LVQQRVPLEE TAFSGWRRDD
HAIAHKDGDY FRVIGVSVRA SSREVSSWSQ PLLAPVGPGL AAFVTRRIRG VLHVLLHART
EAGLLNGPEM APTVQCRPLN YRAVPAEYRP AYLDYVLSAD PGRIRYDTLQ SEEGGRFHHA
ENRYVVVEAE DDFPVEVPRD FRWLTLHQIL ALLHHSNYVN VEARSLVACI QALS
