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Database: UniProt
Entry: A0A2P4UGE6_9ACTN
LinkDB: A0A2P4UGE6_9ACTN
Original site: A0A2P4UGE6_9ACTN 
ID   A0A2P4UGE6_9ACTN        Unreviewed;       403 AA.
AC   A0A2P4UGE6;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Rhodocoxin reductase {ECO:0000313|EMBL:POM24110.1};
DE            EC=1.18.1.- {ECO:0000313|EMBL:POM24110.1};
GN   Name=thcD {ECO:0000313|EMBL:POM24110.1};
GN   ORFNames=BTM25_27370 {ECO:0000313|EMBL:POM24110.1};
OS   Actinomadura rubteroloni.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM24110.1, ECO:0000313|Proteomes:UP000242367};
RN   [1] {ECO:0000313|EMBL:POM24110.1, ECO:0000313|Proteomes:UP000242367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-2 {ECO:0000313|EMBL:POM24110.1,
RC   ECO:0000313|Proteomes:UP000242367};
RX   PubMed=28463423; DOI=10.1002/chem.201701005;
RA   Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA   Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA   Poulsen M., Beemelmanns C.;
RT   "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT   Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL   Chemistry 23:9338-9345(2017).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:POM24110.1}.
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DR   EMBL; MTBP01000002; POM24110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P4UGE6; -.
DR   Proteomes; UP000242367; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:POM24110.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242367}.
FT   DOMAIN          3..291
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          314..397
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   403 AA;  42029 MW;  6792CCB9FC06FECE CRC64;
     MDRVIIVGGG LAGTRAAEAL RARGFAGALT LVGAEARRPY DRPPLSKAVL AGDADTSELT
     ADWDALRCDL LLGERATGLR PAPGRGGTLA TTAGDLPFDG LVIATGAVPV LLPGPGRQHV
     LRTHEDAHEL RGHLRPGARI VIVGAGWIGA EVATAAAKKG CRVTVAEAGE APLVQALGAD
     LGARTAPWYA AAGVELRTGV RVASVEDDGL LLAGGERLAA DAVVTGIGVR PEVGWLDGSG
     LDVELGVLAD PSLRASIGGV PRPDIVAVGD CAAWWSNRHG RRVLAEHWDA ALNAPEVAAA
     TLLGADAVYD AIPYFWSEQF GHMVQYLGRH EDAERRIDRG DPAGPSWSTV WLTGDRVDAV
     LAVDRPRDLV QARRLMAAGT PVDPVIAADP DIPLRQAVRV RPS
//
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