PTLF_STRAW
ID PTLF_STRAW Reviewed; 270 AA.
AC Q82IY9;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=1-deoxy-11-beta-hydroxypentalenate dehydrogenase;
DE EC=1.1.1.340;
DE AltName: Full=Neopentalenolactone biosynthesis protein F;
GN Name=ptlF; OrderedLocusNames=SAV_2993;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=17178094; DOI=10.1016/j.abb.2006.11.016;
RA You Z., Omura S., Ikeda H., Cane D.E.;
RT "Pentalenolactone biosynthesis: Molecular cloning and assignment of
RT biochemical function to PtlF, a short-chain dehydrogenase from Streptomyces
RT avermitilis, and identification of a new biosynthetic intermediate.";
RL Arch. Biochem. Biophys. 459:233-240(2007).
RN [4]
RP PATHWAY.
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=21250661; DOI=10.1021/bi1019786;
RA Seo M.J., Zhu D., Endo S., Ikeda H., Cane D.E.;
RT "Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger
RT monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the
RT final steps of the biosynthesis of pentalenolactone and
RT neopentalenolactone.";
RL Biochemistry 50:1739-1754(2011).
CC -!- FUNCTION: Catalyzes the oxidation of 1-deoxy-11-beta-hydroxypentalenic
CC acid to 1-deoxy-11-oxopentalenic acid in the biosynthesis of
CC neopentalenolactone antibiotic. {ECO:0000269|PubMed:17178094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxy-11beta-hydroxypentalenate + NAD(+) = 1-deoxy-11-
CC oxopentalenate + H(+) + NADH; Xref=Rhea:RHEA:34559,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:70779, ChEBI:CHEBI:70780; EC=1.1.1.340;
CC Evidence={ECO:0000269|PubMed:17178094};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 uM for 1-deoxy-11-beta-hydroxypentalenic acid
CC {ECO:0000269|PubMed:17178094};
CC KM=25 uM for NAD {ECO:0000269|PubMed:17178094};
CC Note=kcat is 0.65 sec(-1).;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:17178094};
CC -!- PATHWAY: Antibiotic biosynthesis; neopentalenolactone biosynthesis.
CC {ECO:0000269|PubMed:21250661}.
CC -!- MISCELLANEOUS: S.avermitilis does not produce pentalenolactone itself
CC in vivo but instead a group of new metabolites that are
CC neopentalenolactone derivatives. {ECO:0000305|PubMed:21250661}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BA000030; BAC70704.1; -; Genomic_DNA.
DR RefSeq; WP_010984424.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82IY9; -.
DR SMR; Q82IY9; -.
DR STRING; 227882.SAV_2993; -.
DR EnsemblBacteria; BAC70704; BAC70704; SAVERM_2993.
DR KEGG; sma:SAVERM_2993; -.
DR eggNOG; COG0300; Bacteria.
DR HOGENOM; CLU_010194_2_1_11; -.
DR OMA; CPGRVDT; -.
DR OrthoDB; 1582456at2; -.
DR BioCyc; MetaCyc:MON-16841; -.
DR BRENDA; 1.1.1.340; 5980.
DR UniPathway; UPA01021; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901336; P:lactone biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..270
FT /note="1-deoxy-11-beta-hydroxypentalenate dehydrogenase"
FT /id="PRO_0000421997"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 28161 MW; 296CBE8898DBCA75 CRC64;
MHLQPSTAVV TGAASGIGFA LSARLAQAGA RVVMTDIAGD GLAGAVEELA AHGADVTAVV
ADLTDPAAVQ ELADTAFGRL GDIDVVCNNA GVVGPVGMPL WSVPLDEMHA VFDVNYWAHV
HVARAFVPRL LDSGRPSHLV QTASMSAFVV GAGTASYAAS KHADLAAARS LRADLDGTPV
RVSVLCPGRV DTPMTRGLVA PRNATGNTTI SADEAADAVW NALGSDRFYI FTNADAQTRL
GDQFNDVWRH LAREKYWTES SSPSVNSSRP
