(data stored in SCRATCH zone)

SWISSPROT: Q13DX2_RHOPS

ID   Q13DX2_RHOPS            Unreviewed;       607 AA.
AC   Q13DX2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN   OrderedLocusNames=RPD_0479 {ECO:0000313|EMBL:ABE37717.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37717.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37717.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37717.1,
RC   ECO:0000313|Proteomes:UP000001818};
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.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|RuleBase:RU362051};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362051};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (bacterial route): step 1/1.
CC       {ECO:0000256|RuleBase:RU362051}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU362051}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU362051}; Cytoplasmic side
CC       {ECO:0000256|RuleBase:RU362051}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|RuleBase:RU362051}.
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DR   EMBL; CP000283; ABE37717.1; -; Genomic_DNA.
DR   RefSeq; WP_011500905.1; NC_007958.1.
DR   STRING; 316057.RPD_0479; -.
DR   EnsemblBacteria; ABE37717; ABE37717; RPD_0479.
DR   KEGG; rpd:RPD_0479; -.
DR   eggNOG; ENOG4105C00; Bacteria.
DR   eggNOG; COG1053; LUCA.
DR   HOGENOM; HOG000160475; -.
DR   KO; K00239; -.
DR   OMA; GDSPWEH; -.
DR   OrthoDB; 153138at2; -.
DR   BioCyc; RPAL316057:RPD_RS02465-MONOMER; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 3.90.700.10; -; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   SUPFAM; SSF46977; SSF46977; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF56425; SSF56425; 1.
DR   TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13DX2.
DR   SWISS-2DPAGE; Q13DX2.
KW   Cell inner membrane {ECO:0000256|RuleBase:RU362051};
KW   Cell membrane {ECO:0000256|RuleBase:RU362051};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Electron transport {ECO:0000256|RuleBase:RU362051};
KW   FAD {ECO:0000256|RuleBase:RU362051};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362051};
KW   Membrane {ECO:0000256|RuleBase:RU362051};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362051,
KW   ECO:0000313|EMBL:ABE37717.1};
KW   Transport {ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN       24    419       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      474    607       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
SQ   SEQUENCE   607 AA;  65976 MW;  7B5CA2CED896F890 CRC64;
     MAANGNGAPA VNGHAYPIED HVYDVVVVGA GGAGLRAVVG CSEAGLRTAC ITKVFPTRSH
     TVAAQGGISA ALGNMHKDDW RWHMYDTVKG SDWLGDQDSI EYMVRNAPEA VYELEHWGVP
     FSRTEEGKIY QRPFGGMTME FGKGQAQRTC AAADRTGHAM LHTMYGQALR HAAEFYIEFF
     AIDLIMDDQG CCRGVIALKL DDGTLHRFRA QTTILATGGY GRAYASCTSA HTCTGDGGAM
     ALRAGLPLQD MEFVQFHPTG IYGSGCLVTE GARGEGGYLV NSEGERFMER YAPSAKDLAS
     RDVVSRAMTI EMREGRGVGK KKDHIFLHLD HLAPEVLAER LPGISESARI FAGVDVTREP
     IPILPTVHYN MGGIPTNFRG EVVTKKEGDD NAVVPGLMAI GEAACVSVHG ANRLGSNSLI
     DLVVFGRAAA LRCAEKLTIN GKQPELPADS ADGTLSRLDK YRYASGGTPT AKLRESMQQV
     MQNNCAVFRT GEVLSEGKDL IRKVHGGVGD IGVSDRSLVW NSDLVETLEF DNLIIQAVVT
     MNSAANRTES RGAHAREDFP DRDDKQWMKH TLAWIGDDGD TTIDYRPVHD YTMTNDVQYI
     PPKPRVY
//

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