ID A0A0D6T8Y7_9RHOB Unreviewed; 715 AA.
AC A0A0D6T8Y7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KIX16645.1};
GN ORFNames=SY26_15040 {ECO:0000313|EMBL:KIX16645.1};
OS Paracoccus sp. 228.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX16645.1, ECO:0000313|Proteomes:UP000032743};
RN [1] {ECO:0000313|EMBL:KIX16645.1, ECO:0000313|Proteomes:UP000032743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=361 {ECO:0000313|EMBL:KIX16645.1,
RC ECO:0000313|Proteomes:UP000032743};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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:KIX16645.1}.
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DR EMBL; JYGY01000005; KIX16645.1; -; Genomic_DNA.
DR RefSeq; WP_046001203.1; NZ_JYGY01000005.1.
DR AlphaFoldDB; A0A0D6T8Y7; -.
DR STRING; 1192054.SY26_15040; -.
DR PATRIC; fig|1603292.4.peg.3221; -.
DR OrthoDB; 9776382at2; -.
DR Proteomes; UP000032743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF09335; SNARE_assoc; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000032743};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..182
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 237..559
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 581..687
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 715 AA; 77145 MW; 5796E6FAAE4EB20B CRC64;
MTRPLLLILV AALVLAGSWL LGGQDVTLQS LRGHLAAVAE YQQQRPVLVA ALFAAAYVAI
TALSLPIAVW LTLAGGALFG FWAGLAIVSF ASAIGATLAF LAARYLLRDW VRARLGARAK
GIETGLARDG AFYLFSLRLI PVMPFFATNL LMGLTPIRTR TFYWVSQLGM LAGTAVYVNA
GTQLAALHSL SEIVSPPLLA SFAALAVFPW IARAIVGILR RRRVYAGWTR PRRFDRNLVV
IGAGSAGLVS AYIAAATKAK VTLIEAGAMG GDCLNHGCVP SKALIRSATV AHQMRHAARF
GLADTPPAVP FRAVMDRIRR VIADIAPHDS VDRYAGLGVD VLQGHARLID PWTVAVTDPQ
GAERRLTTRA IIIATGARPV MPPLPGLDLV DPLTSETLWS RLADHDHAPR RLVVLGGGPI
GCELAQAFAR LGSDVTQIEM APRLLMREDP EVSALVADAL RADGVTVLAG HRAIRCGIDG
GRWIEVERDG AARRIGFDQI IVAVGRSARL EGFGLDRLGI ETDRTIVTNA FLQTRFPHIL
AAGDVAGPFQ FTHAASHQAW FASVNALFGT LRRFKVDDRV IPWATFTDPQ IARVGLSETE
ARDRGIAVEV TRYDLADLDR AITDGAARGF VKVLTPPGRD RILGVTIAGD HAGDLIAEFV
LAMKHGLGLN KVLATIHIYP TWAEANKAVA GTWRRAHVNP RLLALVERYH RWRRG
//
