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OXYR_STRR1
ID   OXYR_STRR1              Reviewed;         142 AA.
AC   L8EYU3;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=5a,11a-dehydrotetracycline/5a,11a-dehydrooxytetracycline reductase {ECO:0000303|PubMed:23621493};
DE            EC=1.3.98.4 {ECO:0000269|PubMed:23621493};
DE   AltName: Full=12-dehydrotetracycline dehydrogenase {ECO:0000305};
DE   AltName: Full=Dehydrooxytetracycline dehydrogenase {ECO:0000305};
DE   AltName: Full=F420-dependent C5a-C11a reductase {ECO:0000303|PubMed:23621493};
GN   Name=oxyR {ECO:0000312|EMBL:ELQ83302.1};
GN   ORFNames=SRIM_10931 {ECO:0000312|EMBL:ELQ83302.1};
OS   Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM
OS   4667 / NRRL 2234).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1265868;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10970 / DSM 40260 / JCM 4667 / NRRL 2234;
RX   PubMed=23516198; DOI=10.1128/genomea.00063-13;
RA   Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Liu T.-T., Chu J.,
RA   Kosec G., Petkovic H., Guo M., Kirby R., Hoskisson P.A., Herron P.R.,
RA   Hunter I.S.;
RT   "Draft genome sequence of the oxytetracycline-producing bacterium
RT   Streptomyces rimosus ATCC 10970.";
RL   Genome Announc. 1:E00063-E00063(2013).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBSTRATE SPECIFICITY,
RP   AND PATHWAY.
RC   STRAIN=ATCC 10970 / DSM 40260 / JCM 4667 / NRRL 2234;
RX   PubMed=23621493; DOI=10.1021/ja403516u;
RA   Wang P., Bashiri G., Gao X., Sawaya M.R., Tang Y.;
RT   "Uncovering the enzymes that catalyze the final steps in oxytetracycline
RT   biosynthesis.";
RL   J. Am. Chem. Soc. 135:7138-7141(2013).
CC   -!- FUNCTION: Involved in the biosynthesis of the antibiotics tetracycline
CC       and oxytetracycline. Catalyzes the C(5) reduction of 5a,11a-
CC       dehydrooxytetracycline to yield oxytetracycline as a major product.
CC       Also catalyzes the C(12) reduction of 5a,11a-dehydrotetracycline (12-
CC       dehydrotetracycline) to produce tetracycline as a minor product.
CC       {ECO:0000269|PubMed:23621493}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) + tetracycline
CC         = 5a,11a-dehydrotetracycline + reduced coenzyme F420-(gamma-L-
CC         Glu)(n); Xref=Rhea:RHEA:50384, Rhea:RHEA-COMP:12939, Rhea:RHEA-
CC         COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57522, ChEBI:CHEBI:77932,
CC         ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.3.98.4;
CC         Evidence={ECO:0000269|PubMed:23621493};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) +
CC         oxytetracycline = 5a,11a-dehydrooxytetracycline + reduced coenzyme
CC         F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:50392, Rhea:RHEA-COMP:12939,
CC         Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:133011,
CC         ChEBI:CHEBI:133012, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC         EC=1.3.98.4; Evidence={ECO:0000269|PubMed:23621493};
CC   -!- PATHWAY: Antibiotic biosynthesis; oxytetracycline biosynthesis.
CC       {ECO:0000305|PubMed:23621493}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC       oxytetracycline. {ECO:0000269|PubMed:23621493}.
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; ANSJ01000024; ELQ83302.1; -; Genomic_DNA.
DR   RefSeq; WP_003981035.1; NZ_ANSJ01000024.1.
DR   AlphaFoldDB; L8EYU3; -.
DR   SMR; L8EYU3; -.
DR   EnsemblBacteria; ELQ83302; ELQ83302; SRIM_10931.
DR   GeneID; 66859921; -.
DR   PATRIC; fig|1265868.3.peg.2255; -.
DR   OMA; WNMAGEP; -.
DR   BioCyc; MetaCyc:MON-19944; -.
DR   UniPathway; UPA00926; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.110.10; -; 1.
DR   InterPro; IPR024031; MSMEG_5819/OxyR.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   TIGRFAMs; TIGR04023; PPOX_MSMEG_5819; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Oxidoreductase.
FT   CHAIN           1..142
FT                   /note="5a,11a-dehydrotetracycline/5a,11a-
FT                   dehydrooxytetracycline reductase"
FT                   /id="PRO_0000443521"
SQ   SEQUENCE   142 AA;  15851 MW;  EDB0DF3A41299090 CRC64;
     MPFTQKEITY LRAQGYGRLA TVGAHGEPHN VPVSFEIDEE RGTIEITGRD MGRSRKFRNV
     AKNDRVAFVV DDVPCRDPEV VRAVVIHGTA QALPTGGRER RPHCADEMIR IHPRRIVTWG
     IEGDLSTGVH ARDITAEDGG RR
 
 
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