ID   OXYQ_STRRM              Reviewed;         359 AA.
AC   Q3S8P9;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=4-dedimethylamino-4-oxo-anhydrotetracycline transaminase OxyQ {ECO:0000303|PubMed:18422316};
DE            EC=2.6.1.- {ECO:0000305|PubMed:18422316};
DE   AltName: Full=PLP-dependent aminotransferase OxyQ {ECO:0000303|PubMed:18422316};
DE   AltName: Full=Reductive transaminase oxyQ {ECO:0000303|PubMed:18422316};
GN   Name=oxyQ {ECO:0000303|PubMed:16597959};
OS   Streptomyces rimosus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16597959; DOI=10.1128/aem.72.4.2573-2580.2006;
RA   Zhang W., Ames B.D., Tsai S.C., Tang Y.;
RT   "Engineered biosynthesis of a novel amidated polyketide, using the
RT   malonamyl-specific initmguPCPB_SPHCRiation module from the oxytetracycline
RT   polyketide synthase.";
RL   Appl. Environ. Microbiol. 72:2573-2580(2006).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=18422316; DOI=10.1021/ja800951e;
RA   Zhang W., Watanabe K., Cai X., Jung M.E., Tang Y., Zhan J.;
RT   "Identifying the minimal enzymes required for anhydrotetracycline
RT   biosynthesis.";
RL   J. Am. Chem. Soc. 130:6068-6069(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of the tetracycline antibiotic,
CC       oxytetracycline. Catalyzes the conversion of 4-dedimethylamino-4-
CC       oxoanhydrotetracycline to yield 4-amino-4-
CC       de(dimethylamino)anhydrotetracycline (4-amino-ATC).
CC       {ECO:0000269|PubMed:18422316}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:O84395};
CC   -!- PATHWAY: Antibiotic biosynthesis; oxytetracycline biosynthesis.
CC       {ECO:0000305|PubMed:18422316}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce the
CC       tetracycline intermediate anhydrotetracycline (ATC).
CC       {ECO:0000269|PubMed:18422316}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; DQ143963; AAZ78340.1; -; Genomic_DNA.
DR   RefSeq; WP_003981034.1; NZ_SADA01000149.1.
DR   AlphaFoldDB; Q3S8P9; -.
DR   SMR; Q3S8P9; -.
DR   GeneID; 66859922; -.
DR   KEGG; ag:AAZ78340; -.
DR   OMA; LCHDHAY; -.
DR   UniPathway; UPA00926; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR019880; OxyQ.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03539; DapC_actino; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..359
FT                   /note="4-dedimethylamino-4-oxo-anhydrotetracycline
FT                   transaminase OxyQ"
FT                   /id="PRO_0000442359"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         91..92
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         155
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         186
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         216..218
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         227
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
FT   MOD_RES         219
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:O84395"
SQ   SEQUENCE   359 AA;  38487 MW;  8A6089F0B305BE57 CRC64;
     MRELPEFPWD VLLPYKKRAA AHPDGLVNLA LGEPVDATPD VLRDALAAAT DAPGYPPTEG
     TPALREAAAA WLRRRLGVTV DPSAVLPAVG TKELIAWLPA MLGTGPGDTV AFPRLAFPTF
     DVSARLAGAR GRPVDSPLEL GSEPVKVVWL NSPSNPEGRV LSVPELREIV AWARDRGAVL
     VNDECYIEYG WDRRPVSLLD SAVCGGSHDG LLAVHSLSKR SNLAGYRAGV CSGDPALIGR
     LLQVRKHAGH AVPAPVQAAM VAALEDDAHV ERQRDRYAYR RRVLRTALEG AGFRVEHSEG
     GLFLWATRGE PCWPAVQKLA DLGILVAPGA FYGEAGEQYV RIAFTATDER IAAAAARLT