ID Q07R09_RHOP5 Unreviewed; 405 AA.
AC Q07R09;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ABJ05625.1};
GN OrderedLocusNames=RPE_1676 {ECO:0000313|EMBL:ABJ05625.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ05625.1};
RN [1] {ECO:0000313|EMBL:ABJ05625.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ05625.1};
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., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000463; ABJ05625.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07R09; -.
DR STRING; 316055.RPE_1676; -.
DR KEGG; rpe:RPE_1676; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_5; -.
DR OrthoDB; 7809559at2; -.
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;
FT DOMAIN 5..301
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..403
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 405 AA; 43534 MW; B6D83BFC7E221FD7 CRC64;
MTGPVVIVGA GHAGFQVAVS LRQAKYAGRI LLLNDEKHLP YQRPPLSKAY LKGEGAPDSL
MFRPQKFFED QTIELIYDSA KAIDRKAKTV RLGSGTTLGY DHLVIATGAR NRLLDVPNAT
LDDVLYLRTM DESEVVRQRM PQRKHVVVVG AGFIGLEFAA TARSKGLEVD VVELAPRVMA
RAVTPEISAY FHDRHTAAGI RIHYGVRATA IEATDGKVSG VALSDGRHLP ADLVVVGVGV
IPNVELAAEA DLPVASGIIV NEQLLTADPN VSAIGDCSLF ASHRFGELMR LESVQNATDQ
ARCVAARLTG DAKIYDGYPW FWSDQGDDKL QIAGLTAGFD QVVVRGSVAE RSFSAFCYKA
GQLIGIESVN RASDHVLGRK LLPTGGTIPP EQAADLSLDL KKALA
//
