ID Q218H7_RHOPB Unreviewed; 409 AA.
AC Q218H7;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ABD87209.1};
GN OrderedLocusNames=RPC_1647 {ECO:0000313|EMBL:ABD87209.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD87209.1};
RN [1] {ECO:0000313|EMBL:ABD87209.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD87209.1};
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., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-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; CP000301; ABD87209.1; -; Genomic_DNA.
DR AlphaFoldDB; Q218H7; -.
DR STRING; 316056.RPC_1647; -.
DR KEGG; rpc:RPC_1647; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_0_5; -.
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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 4: Predicted;
FT DOMAIN 9..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 324..407
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 409 AA; 44224 MW; 9DF286042DB9436E CRC64;
MSMTMTGPVL IVGAGHAGFQ VAVSLRQAKF AGRIVLINDE KHLPYQRPPL SKAYLKGEGA
PDSLMFRPEK FFTEQNIELV SDRVVSIDRA ARKLLLGSGN SLDYGHLVLA TGARNRLLDV
PNATLEDVLY LRTMDESELV RQRMPLRKHA VVIGAGFIGL EFAATARSKG LEVDVLELAP
RVMSRAVTPE ISAYFHDRHT AAGIRIHYGV RATEIEATDG KVSGVSLSDG RRIEADLVVV
GVGVIPNVEL AAAAELPTAS GVIVNEQLLT ADPNVSAIGD CALFASERFG ELMRLESVQN
ATDQARCVAA RLTGDAKTYD GYPWFWSDQG DDKLQIAGLT AGFDQVVVRG SVAERSFSAF
CYKDGKLIGI ESVNRAADHV FGRKMLPTGR SITPEQAVDL SFDLKKALA
//
