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Database: UniProt
Entry: B6B2H5_9RHOB
LinkDB: B6B2H5_9RHOB
Original site: B6B2H5_9RHOB 
ID   B6B2H5_9RHOB            Unreviewed;       403 AA.
AC   B6B2H5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Rhodocoxin reductase {ECO:0000313|EMBL:EDZ42321.1};
GN   ORFNames=RB2083_1836 {ECO:0000313|EMBL:EDZ42321.1};
OS   Rhodobacteraceae bacterium HTCC2083.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=314270 {ECO:0000313|EMBL:EDZ42321.1, ECO:0000313|Proteomes:UP000005746};
RN   [1] {ECO:0000313|Proteomes:UP000005746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2083 {ECO:0000313|Proteomes:UP000005746};
RX   PubMed=21036993; DOI=10.1128/JB.01268-10;
RA   Kang I., Vergin K.L., Oh H.M., Choi A., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of strain HTCC2083, a novel member of the marine clade
RT   Roseobacter.";
RL   J. Bacteriol. 193:319-320(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; DS995276; EDZ42321.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6B2H5; -.
DR   STRING; 314270.RB2083_1836; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_0_5; -.
DR   OrthoDB; 7809559at2; -.
DR   Proteomes; UP000005746; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; PR00411; PNDRDTASEI.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005746}.
FT   DOMAIN          4..298
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          317..401
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
FT   COILED          281..308
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   403 AA;  43136 MW;  873638C3CB11B82A CRC64;
     MAHFVIIGAG QAGSSLVAKL RSSGFEGEIT LIGEEHVPPY QRPPLSKAYL LGDMALERLF
     LRPESFYADQ HITLKMGTAV TSIDTAKREV HLGDEVISYD QLALTTGSHA NTLPASIGGA
     LDGVFTVRTL ADVDAMADHF NAGKRALIVG GGYIGLEAAA VARKMGVEVT VVEMAERILQ
     RVAAPDTSDY FRALHQSHGV KIFEGVGLKS LNGEGYVSGA TLANGTELDV DFVIVGVGIT
     PNASLAEKAG LTIENGIAVN EQGCTSDPNI WSAGDCASFD LRGARRRLES VQNAIDQAEA
     VAENMLGAGK TYTPKPWFWS DQYDVKLQIA GLNIGYDSVV ARRDTNSPAI SFWYYKDDTL
     LAVDAMNDPR NYMIGKRLIE AGKSPTPDVI ANPDTDMKAL LKA
//
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