SNOAL_STRNO
ID SNOAL_STRNO Reviewed; 134 AA.
AC Q9RN59;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Nogalonic acid methyl ester cyclase {ECO:0000303|PubMed:10639368};
DE Short=NAME cyclase {ECO:0000303|PubMed:10639368};
DE EC=5.5.1.26 {ECO:0000269|PubMed:10639368, ECO:0000269|PubMed:15071504};
DE AltName: Full=Polyketide cyclase SnoaL {ECO:0000303|PubMed:15071504};
GN Name=snoaL {ECO:0000303|PubMed:10639368};
OS Streptomyces nogalater.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=38314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 27451 / DSM 40546 / JCM 4553 / NBRC 13445 / NCIMB 9489 / VKM
RC Ac-1290;
RX PubMed=10639368; DOI=10.1128/aac.44.2.396-399.2000;
RA Torkkell S., Kunnari T., Palmu K., Hakala J., Mantsala P., Ylihonko K.;
RT "Identification of a cyclase gene dictating the C-9 stereochemistry of
RT anthracyclines from Streptomyces nogalater.";
RL Antimicrob. Agents Chemother. 44:396-399(2000).
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=15159574; DOI=10.1107/s090744490400705x;
RA Sultana A., Kallio P., Jansson A., Niemi J., Maentsaelae P., Schneider G.;
RT "Crystallization and preliminary crystallographic data of SnoaL, a
RT polyketide cyclase in nogalamycin biosynthesis.";
RL Acta Crystallogr. D 60:1118-1120(2004).
RN [3] {ECO:0007744|PDB:1SJW}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH NOGALAVIKETONE,
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF PHE-5; GLN-95 AND ASP-111.
RX PubMed=15071504; DOI=10.1038/sj.emboj.7600201;
RA Sultana A., Kallio P., Jansson A., Wang J.S., Niemi J., Mantsala P.,
RA Schneider G.;
RT "Structure of the polyketide cyclase SnoaL reveals a novel mechanism for
RT enzymatic aldol condensation.";
RL EMBO J. 23:1911-1921(2004).
CC -!- FUNCTION: Involved in the biosynthesis of the aromatic polyketide
CC antibiotic nogalamycin. Catalyzes the formation of nogalaviketone from
CC nogalonic acid methyl ester (NAME), the last ring-closure step in the
CC biosynthesis of nogalamycin. {ECO:0000269|PubMed:10639368,
CC ECO:0000269|PubMed:15071504}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nogalaviketone = methyl nogalonate; Xref=Rhea:RHEA:44356,
CC ChEBI:CHEBI:84342, ChEBI:CHEBI:84345; EC=5.5.1.26;
CC Evidence={ECO:0000269|PubMed:10639368, ECO:0000269|PubMed:15071504};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:44358;
CC Evidence={ECO:0000269|PubMed:10639368, ECO:0000269|PubMed:15071504};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:10639368}.
CC -!- SUBUNIT: Homotetramer (PubMed:15159574, PubMed:15071504). Dimer of
CC dimers (PubMed:15071504). {ECO:0000269|PubMed:15071504,
CC ECO:0000269|PubMed:15159574}.
CC -!- SIMILARITY: Belongs to the polyketide cyclase DnrD family.
CC {ECO:0000305}.
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DR EMBL; AF187532; AAF01813.1; -; Genomic_DNA.
DR PDB; 1SJW; X-ray; 1.35 A; A=1-134.
DR PDBsum; 1SJW; -.
DR AlphaFoldDB; Q9RN59; -.
DR SMR; Q9RN59; -.
DR DrugBank; DB04064; Nogalaviketone.
DR KEGG; ag:AAF01813; -.
DR BRENDA; 5.5.1.26; 13766.
DR EvolutionaryTrace; Q9RN59; -.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0030638; P:polyketide metabolic process; IEA:InterPro.
DR InterPro; IPR009959; Cyclase_SnoaL-like.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR PANTHER; PTHR38436; PTHR38436; 1.
DR Pfam; PF07366; SnoaL; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Isomerase.
FT CHAIN 1..134
FT /note="Nogalonic acid methyl ester cyclase"
FT /id="PRO_0000452283"
FT ACT_SITE 111
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:15071504"
FT BINDING 95
FT /ligand="nogalaviketone"
FT /ligand_id="ChEBI:CHEBI:84342"
FT /evidence="ECO:0000269|PubMed:15071504,
FT ECO:0007744|PDB:1SJW"
FT MUTAGEN 5
FT /note="F->Y: 20-fold decrease in specific activity."
FT /evidence="ECO:0000269|PubMed:15071504"
FT MUTAGEN 95
FT /note="Q->A: 6-fold decrease in specific activity."
FT /evidence="ECO:0000269|PubMed:15071504"
FT MUTAGEN 111
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15071504"
FT HELIX 1..7
FT /evidence="ECO:0007829|PDB:1SJW"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1SJW"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:1SJW"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:1SJW"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:1SJW"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:1SJW"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1SJW"
FT STRAND 90..102
FT /evidence="ECO:0007829|PDB:1SJW"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:1SJW"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:1SJW"
SQ SEQUENCE 134 AA; 15505 MW; 342F385C982943FB CRC64;
MVSAFNTGRT DDVDEYIHPD YLNPATLEHG IHTGPKAFAQ LVGWVRATFS EEARLEEVRI
EERGPWVKAY LVLYGRHVGR LVGMPPTDRR FSGEQVHLMR IVDGKIRDHR DWPDFQGTLR
QLGDPWPDDE GWRP
