ID   O33942_SACER            Unreviewed;       401 AA.
AC   O33942;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   19-JAN-2010, entry version 38.
DE   SubName: Full=EryCIV;
DE   SubName: Full=Putative aminotransferase-dehydrase;
GN   Name=eryCIV; Synonyms=EryCIV;
OS   Saccharopolyspora erythraea (Streptomyces erythraeus).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Pseudonocardineae; Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=1836;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL 2338;
RX   MEDLINE=98015410; PubMed=9353926;
RA   Summers R.G., Donadio S., Staver M.J., Wendt-Pienkowski E.,
RA   Hutchinson C.R., Katz L.;
RT   "Sequencing and mutagenesis of genes from the erythromycin
RT   biosynthetic gene cluster of Saccharopolyspora erythraea that are
RT   involved in L-mycarose and D-desosamine production.";
RL   Microbiology 143:0-0(0).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL 2338;
RA   Summers R.G., Staver M.J., Donadio S., Wendt-Pienkowski E.,
RA   Hutchinson C.R., Katz L.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL2338;
RX   MEDLINE=98055166; PubMed=9393448; DOI=10.1007/s004380050566;
RA   Gaisser S., Bohm G.A., Cortes J., Leadlay P.F.;
RT   "Analysis of seven genes from the eryAI-eryK region of the
RT   erythromycin biosynthetic gene cluster in Saccharopolyspora
RT   erythraea.";
RL   Mol. Gen. Genet. 256:239-251(1997).
CC   -!- SIMILARITY: Belongs to the degT/dnrJ/eryC1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U77459; AAB84075.1; -; Genomic_DNA.
DR   EMBL; Y11199; CAA72084.1; -; Genomic_DNA.
DR   RefSeq; YP_001102983.1; -.
DR   HSSP; Q8ZNF3; 1MDZ.
DR   SMR; O33942; 4-391.
DR   GeneID; 4940577; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   Aminotransferase; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   401 AA;  43347 MW;  F310354E39450C44 CRC64;
     MKRALTDLAI FGGPEAFLHT LYVGRPTVGD RERFFARLEW ALNNNWLTNG GPLVREFEGR
     VADLAGVRHC VATCNATVAL QLVLRASDVS GEVVMPSMTF AATAHAASWL GLEPVFCDVD
     PETGLLDPEH VASLVTPRTG AIIGVHLWGR PAPVEALEKI AAEHQVKLFF DAAHALGCTA
     GGRPVGAFGN AEVFSFHATK AVTSFEGGAI VTDDGLLADR IRAMHNFGIA PDKLVTDVGT
     NGKMSECAAA MGLTSLDAFA ETRVHNRLNH ALYSDELRDV RGISVHAFDP GEQNNYQYVI
     ISVDSAATGI DRDQLQAILR AEKVVAQPYF SPGCHQMQPY RTEPPLRLEN TEQLSDRVLA
     LPTGPAVSSE DIRRVCDIIR LAATSGELIN AQWDQRTRNG S
//

ID   O68842_STRAT            Unreviewed;       368 AA.
AC   O68842;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 2.
DT   19-JAN-2010, entry version 33.
DE   SubName: Full=Aminotransferase;
GN   Name=oleN2;
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=98343801; PubMed=9680207;
RX   DOI=10.1046/j.1365-2958.1998.00880.x;
RA   Quiros L.M., Aguirrezabalaga I., Olano C., Mendez C., Salas J.A.;
RT   "Two glycosyltransferases and a glycosidase are involved in
RT   oleandomycin modification during its biosynthesis by Streptomyces
RT   antibioticus.";
RL   Mol. Microbiol. 28:1177-1185(1998).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF055579; AAD55458.1; -; Genomic_DNA.
DR   PIR; T51111; T51111.
DR   HSSP; Q8ZNF3; 1MDO.
DR   SMR; O68842; 3-362.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   Aminotransferase; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   368 AA;  39602 MW;  7911658830FA0C3F CRC64;
     MDVPFLDLRA AYLELKHDID AATGRVLDSG RYLLGPELAA FETEWAAYCG ARHCVAVGSG
     CDALELALRA MDIGPGDEVI VPAHTFAATW LAVSATGAEP VAVEPEPATF TLDPERVEAA
     ITSRTRVILP VHLYGHPADL AALSEVAERH GVRILEDAAQ AHGAQAYGRR VGAWSTTAFS
     FYPGKNLGGF GDGGAVVTDD AELAERVRLL RNYGSREKYR HEVRATNFRL DELQAAVLRV
     KLAHLDAWTE RRAAVAARYL DGLAGLDGIV LPRPAPWADP VWHLFVIRSA DRSALRERLA
     AAGVETLIHY PVPVHRSEAY AGSRQAARAQ PVAERLAREV LSLPIGPHLS DDAVKAVIEA
     VRGAVAAC
//

ID   Q9ZGH4_9ACTO            Unreviewed;       379 AA.
AC   Q9ZGH4;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   19-JAN-2010, entry version 29.
DE   SubName: Full=Transaminase;
GN   Name=desV;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF079762; AAC68680.1; -; Genomic_DNA.
DR   PDB; 2OGA; X-ray; 2.05 A; A/B/C/D=1-379.
DR   PDB; 2OGE; X-ray; 2.05 A; A/B/C/D=1-379.
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   379 AA;  41184 MW;  1A4FD0F4E76DCCDB CRC64;
     MSSRAETPRV PFLDLKAAYE ELRAETDAAI ARVLDSGRYL LGPELEGFEA EFAAYCETDH
     AVGVNSGMDA LQLALRGLGI GPGDEVIVPS HTYIASWLAV SATGATPVPV EPHEDHPTLD
     PLLVEKAITP RTRALLPVHL YGHPADMDAL RELADRHGLH IVEDAAQAHG ARYRGRRIGA
     GSSVAAFSFY PGKNLGCFGD GGAVVTGDPE LAERLRMLRN YGSRQKYSHE TKGTNSRLDE
     MQAAVLRIRL AHLDSWNGRR SALAAEYLSG LAGLPGIGLP VTAPDTDPVW HLFTVRTERR
     DELRSHLDAR GIDTLTHYPV PVHLSPAYAG EAPPEGSLPR AESFARQVLS LPIGPHLERP
     QALRVIDAVR EWAERVDQA
//