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Database: UniProt
Entry: A4TD95_MYCGI
LinkDB: A4TD95_MYCGI
Original site: A4TD95_MYCGI 
ID   A4TD95_MYCGI            Unreviewed;       509 AA.
AC   A4TD95;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ABP46968.1};
GN   OrderedLocusNames=Mflv_4499 {ECO:0000313|EMBL:ABP46968.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP46968.1};
RN   [1] {ECO:0000313|EMBL:ABP46968.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46968.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP46968.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46968.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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DR   EMBL; CP000656; ABP46968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TD95; -.
DR   STRING; 350054.Mflv_4499; -.
DR   KEGG; mgi:Mflv_4499; -.
DR   eggNOG; COG2072; Bacteria.
DR   HOGENOM; CLU_032067_2_0_11; -.
DR   OrthoDB; 5168853at2; -.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43872; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR   PANTHER; PTHR43872:SF1; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02570)-RELATED; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
SQ   SEQUENCE   509 AA;  57622 MW;  52FAF304C04EEEAA CRC64;
     MDQLYPETES TDVLIVGAGI SGIGAAYRIQ ERNPQLTYTV LERRSRIGGT WDLHRYPGIR
     SDSDIFTLSF PWEPWDRPEN VADGEDIRQY LVDAARKHGI DRHIHFDTRV LSADWDSTAD
     VWTVRTECNG VPRTYRTRFL FFGTGYYDYD NPYRPEFPGL ESFEGPVVHP QHWPEDLDCT
     GKKVAVIGSG ATAISMIPAL AESAERVTMV QRSPTYLLSG QRINPVVNLL RKVPPRKLGY
     RLAWLYNVLF IVAVYGVARK APRISRRLIR AVAKHYLPEG YPVDTHFKPR YDPWDQRLCL
     ILSGDFYDAI ARGRAEVVTD EIDHIDAHGL VLKSGRRIDA DVLVTATGLQ LQALGGIEIS
     IDGTEVKPAD RFVYKEHLLE DVPNLAWCVG YINASWTLRA DLTARAVAKL LAHMDSHGYT
     HAYPHLGGVP MEEKPAWNIN AGYVHRAPHV LPKSGTHRPW NVRHNYVLDA VDQRFDRIDE
     SMVFGRVSPK LHSSSEMSSE DLLERNFGA
//
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