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}.
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; 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
//