ID   Q9RR26_STRAT            Unreviewed;       393 AA.
AC   Q9RR26;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   19-JAN-2010, entry version 30.
DE   SubName: Full=Dehydratase;
GN   Name=oleNI;
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 11891;
RX   MEDLINE=20233594; PubMed=10770761;
RX   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   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 11891;
RA   Quiros L.M., Aguirrezabalaga I., Olano C., Mendez C., Salas J.A.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the degT/dnrJ/eryC1 family.
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DR   EMBL; AF055579; AAD55456.1; -; Genomic_DNA.
DR   PIR; T51108; T51108.
DR   HSSP; Q8ZNF3; 1MDZ.
DR   SMR; Q9RR26; 4-390.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate.
SQ   SEQUENCE   393 AA;  42674 MW;  EA8CF62F893FBC64 CRC64;
     MKRGVHDLAL FGGDAAFLQP LYMGRPNTGD RKRLLDRLEW ALDNRWLTNG GPLVREFEQR
     IADLAGVRNC VATCNATAGL QLLLREAEVT GEVIMPSMTF VATAHAVRWL GLRPVFCDID
     PDTGCLDPKL VEAAVTPRTG AILGVHLWGR PSRVDELAAI AAEHGLKLFY DAAHALGCTS
     RQRRLGSFGD AEVFSFHATK VVNSFEGGGI VTDDDTRAER LRALHNFGLG HDGVGAGINA
     KMSEAAAAMG LTSLEAFADA VASNRANYEL YRQELSGLPG VRLIDYDPAE RNNYHYVIAL
     IDAGVTGLHR DLLLTLLRAE NVVAQPYFSP GCHQREPYRT EHPVSLPHTE HLAEQVIALP
     TGPAVSREDI RRVCDIIRVA AAHGPRITAQ AGA
//

ID   Q9ZGH0_9ACTO            Unreviewed;       415 AA.
AC   Q9ZGH0;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   19-JAN-2010, entry version 27.
DE   SubName: Full=4-dehydrase;
GN   Name=desI;
OS   Streptomyces venezuelae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=54571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC15439;
RX   MEDLINE=98445333; PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA   Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT   "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT   venezuelae: architecture of metabolic diversity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
CC   -!- SIMILARITY: Belongs to the degT/dnrJ/eryC1 family.
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DR   EMBL; AF079762; AAC68684.1; -; Genomic_DNA.
DR   PDB; 2PO3; X-ray; 2.10 A; A/B=1-415.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
PE   1: Evidence at protein level;
KW   Pyridoxal phosphate.
SQ   SEQUENCE   415 AA;  44292 MW;  6B3D044A1207C443 CRC64;
     MKSALSDLAF FGGPAAFDQP LLVGRPNRID RARLYERLDR ALDSQWLSNG GPLVREFEER
     VAGLAGVRHA VATCNATAGL QLLAHAAGLT GEVIMPSMTF AATPHALRWI GLTPVFADID
     PDTGNLDPDQ VAAAVTPRTS AVVGVHLWGR PCAADQLRKV ADEHGLRLYF DAAHALGCAV
     DGRPAGSLGD AEVFSFHATK AVNAFEGGAV VTDDADLAAR IRALHNFGFD LPGGSPAGGT
     NAKMSEAAAA MGLTSLDAFP EVIDRNRRNH AAYREHLADL PGVLVADHDR HGLNNHQYVI
     VEIDEATTGI HRDLVMEVLK AEGVHTRAYF SPGCHELEPY RGQPHAPLPH TERLAARVLS
     LPTGTAIGDD DIRRVADLLR LCATRGRELT ARHRDTAPAP LAAPQTSTPT IGRSR
//