ID K2JV20_9RHOB Unreviewed; 401 AA.
AC K2JV20;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EKE74149.1};
GN ORFNames=B30_00445 {ECO:0000313|EMBL:EKE74149.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE74149.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE74149.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE74149.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EKE74149.1}.
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DR EMBL; AMRK01000001; EKE74149.1; -; Genomic_DNA.
DR RefSeq; WP_009569989.1; NZ_AMRK01000001.1.
DR AlphaFoldDB; K2JV20; -.
DR STRING; 1208323.B30_00445; -.
DR PATRIC; fig|1208323.3.peg.91; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 7809559at2; -.
DR Proteomes; UP000006762; 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 Reference proteome {ECO:0000313|Proteomes:UP000006762}.
FT DOMAIN 4..298
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 317..399
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 401 AA; 42876 MW; 8245EB4B2155DC8B CRC64;
MSHFIVVGAG QAGQSIVTTL RGQGFDGKIT LIGDEPVPPY QRPPLSKAYL LGDMDLDRLY
LRPLSYYADE TIDLRMGASV TALDPAAKTI TVDGEHLSYD KLALATGSAP RVLPASIGGT
LQGVYTMRTL ADADAIEPEF KEGASVLIVG GGYIGLEAAA VAAKKGLKVT LVEMSDRILQ
RVASKETSDY FRALHQSHGV DLREGVGLET LVGDTRVNAA KLTDGTTLDV DFVIVGVGIT
PNTQLAELAG LVLDNGIMTD RHSCTSNPDI FAAGDCASFP HMGHQMRLES VGNAIDQGAV
VAKNMLGQAV DYTPKPWFWS DQFDVKLQIA GLSTGHDQVV IRETETTRSH WYYKEGALIA
IDAMNDPRGY MVAKRLIEAG KSADPALVAD PATDLKALMR S
//
