ID   CTCQ_KITAU              Reviewed;         191 AA.
AC   S4S3E3;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Flavin reductase (NADH) {ECO:0000303|PubMed:23800859};
DE            EC=1.5.1.36 {ECO:0000305|PubMed:23800859};
GN   Name=ctcQ {ECO:0000303|PubMed:23800859};
GN   ORFNames=B6264_18520 {ECO:0000312|EMBL:ARF80632.1},
GN   HS99_0013300 {ECO:0000312|EMBL:OEV33528.1};
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=1894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=F3 {ECO:0000312|EMBL:AEI98660.1};
RX   PubMed=23800859; DOI=10.1016/j.ymben.2013.06.003;
RA   Zhu T., Cheng X., Liu Y., Deng Z., You D.;
RT   "Deciphering and engineering of the final step halogenase for improved
RT   chlortetracycline biosynthesis in industrial Streptomyces aureofaciens.";
RL   Metab. Eng. 19:69-78(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843
RC   / NCIMB 8234 / A-377;
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, assembly and comparative genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DM-1 {ECO:0000312|EMBL:ARF80632.1};
RA   Hu H., Huang H., Min T.;
RT   "TAR cloning and integrated overexpression of 6-demethylchlortetracycline
RT   biosynthetic gene cluster in Streptomyces aureofaciens.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of flavin by NADH. Subsequently, the
CC       reduced flavins is transferred to the tetracycline 7-halogenase CtcP.
CC       {ECO:0000269|PubMed:23800859}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:31303, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:60531, ChEBI:CHEBI:62787; EC=1.5.1.36;
CC         Evidence={ECO:0000305|PubMed:23800859};
CC   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HM627755; AEI98660.1; -; Genomic_DNA.
DR   EMBL; JPRF03000065; OEV33528.1; -; Genomic_DNA.
DR   EMBL; CP020567; ARF80632.1; -; Genomic_DNA.
DR   RefSeq; WP_030282588.1; NZ_LBHA01000099.1.
DR   AlphaFoldDB; S4S3E3; -.
DR   SMR; S4S3E3; -.
DR   STRING; 1894.JOER01000001_gene5208; -.
DR   EnsemblBacteria; ARF80632; ARF80632; B6264_18520.
DR   EnsemblBacteria; OEV33528; OEV33528; HS99_0013300.
DR   KEGG; ag:AEI98660; -.
DR   KEGG; kau:B6264_18520; -.
DR   OMA; AGWIACH; -.
DR   Proteomes; UP000037395; Unassembled WGS sequence.
DR   GO; GO:0036382; F:flavin reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   Gene3D; 2.30.110.10; -; 1.
DR   InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   Pfam; PF01613; Flavin_Reduct; 1.
DR   SMART; SM00903; Flavin_Reduct; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..191
FT                   /note="Flavin reductase (NADH)"
FT                   /id="PRO_0000443995"
FT   BINDING         46..52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJP7"
FT   BINDING         55
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJP7"
FT   BINDING         72..73
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJP7"
FT   BINDING         144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJP7"
FT   BINDING         166..169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SJP7"
SQ   SEQUENCE   191 AA;  19899 MW;  AD05CE24243EF35C CRC64;
     MPPEPLSLPL DLAPGLVDGD TFLSIMGALP TGVTVVTTLG PDGEPYGLTC SAACSVSKAP
     PLLLVCINRD SRVLKALLER GEFAVNVLRG GGESTSARFA APVDDRFRDV RWEPGSAGGV
     PVMSADVVAH AECRVAAALD AGDHTIVIGA VVAGGPRPEV PSPLMYWRRS YARWPVEEDP
     RTAALTLAAE G