(data stored in ACNUC7421 zone)

SWISSPROT: B2UHF4_RALPJ

ID   B2UHF4_RALPJ            Unreviewed;       459 AA.
AC   B2UHF4;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACD29005.1};
GN   OrderedLocusNames=Rpic_3897 {ECO:0000313|EMBL:ACD29005.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29005.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003691}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001069; ACD29005.1; -; Genomic_DNA.
DR   RefSeq; WP_012430044.1; NC_010678.1.
DR   STRING; 402626.Rpic_3897; -.
DR   EnsemblBacteria; ACD29005; ACD29005; Rpic_3897.
DR   GeneID; 6285028; -.
DR   KEGG; rpi:Rpic_3897; -.
DR   PATRIC; fig|402626.5.peg.135; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276709; -.
DR   OMA; VHIIHHN; -.
DR   OrthoDB; 267896at2; -.
DR   BioCyc; RPIC402626:GH94-3901-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2UHF4.
DR   SWISS-2DPAGE; B2UHF4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN        6    312       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      345    450       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     177    184       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    441    441       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      51     51       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     200    200       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     267    267       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     308    308       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     42     47       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   459 AA;  49432 MW;  D96F28E4DD1167DC CRC64;
     MTQRFDAIII GTGQAGPPLA ARLSGAGLKV AIVERGRFGG TCVNTGCIPT KAMVASAYAA
     RMAQRAAEYG VVIDGGVTVD MRRVKARKDE ISGRSSHGVE QWVRGLEHGT VFQGHARFES
     ARAVRVGDEL LEAERIFINV GGRALVPPMP GLDQVPFLTN STMMDVDFLP EHLVVIGGSY
     VGLEFGQMFR RFGSRVTIVE KGPRLIARED EDVSQAVREI LEAEGIDVQV NADCLSVRRD
     GAGVVVGLEC GSGAREVSGS HLLMAVGRVP NTDDLGLDKA GVEIDKRGNI RVDEQLRTNV
     PGIWAMGDCN GRGAFTHTSY NDYEIVAANL LDSDPRKVSD RIQAYAMYID PPLARVGMSL
     TEAKQSGRTL LVGNRPMTRV GRAVEKGESQ GFMRVVVDAQ THEILGASIL GVGGDEAVHS
     ILDVMYAKAP YTTISRAMHI HPTVSELIPT LLQSMEPEQ
//

If you have problems or comments...

PBIL Back to PBIL home page