(data stored in SCRATCH zone)

SWISSPROT: A1AZI7_PARDP

ID   A1AZI7_PARDP            Unreviewed;       600 AA.
AC   A1AZI7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN   OrderedLocusNames=Pden_0569 {ECO:0000313|EMBL:ABL68681.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68681.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-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}.
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; CP000489; ABL68681.1; -; Genomic_DNA.
DR   RefSeq; WP_011746914.1; NC_008686.1.
DR   SMR; A1AZI7; -.
DR   STRING; 318586.Pden_0569; -.
DR   PRIDE; A1AZI7; -.
DR   EnsemblBacteria; ABL68681; ABL68681; Pden_0569.
DR   KEGG; pde:Pden_0569; -.
DR   eggNOG; ENOG4105C00; Bacteria.
DR   eggNOG; COG1053; LUCA.
DR   HOGENOM; HOG000160475; -.
DR   KO; K00239; -.
DR   OMA; GDSPWEH; -.
DR   BioCyc; PDEN318586:G1GW1-577-MONOMER; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZI7.
DR   SWISS-2DPAGE; A1AZI7.
KW   Cell inner membrane {ECO:0000256|RuleBase:RU362051};
KW   Cell membrane {ECO:0000256|RuleBase:RU362051};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
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:ABL68681.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transport {ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT   DOMAIN       12    407       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      462    600       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
SQ   SEQUENCE   600 AA;  65616 MW;  E8446E4FB6D8F829 CRC64;
     MAAYKYETHE YDVVVVGAGG AGLRATLGMA EQGLRTACVT KVFPTRSHTV AAQGGIAASL
     SNMGPDNWQW HMYDTVKGSD WLGDTDAMEY LAREAPKAVY ELEHYGVPFS RTEEGKIYQR
     PFGGHTTEFG EGPPVQRTCA AADRTGHAIL HTLYGQSLKE KAEFFIEYFA LDLIITDGAC
     TGVVCWKLDD GTIHVFNAKM VVLATGGYGR AYFSATSAHT CTGDGGGMVA RAGLPLQDME
     FVQFHPTGIY GSGCLITEGA RGEGGYLTNS EGERFMERYA PTYKDLASRD VVSRCITIEI
     REGRGVGPHK DHMHLNLMHL PPESLAERLP GISESAKIFA GVDVTREPIP ILPTVHYNMG
     GIPTNYWGEV LNPTQDNPDQ VFPGLMAVGE AGCASVHGAN RLGSNSLIDL VVFGRAAAIR
     AGQVIDREAQ IPTTNKEQVD KALDRFDRIR NADGSVSTAD LRLEMQRTMQ ADAAVFRTDK
     TLAEGVDKMR VIAGKLSDLK VTDRSLIWNS DLMETLELTN LMPNALATIV AAEARKESRG
     AHAHEDYPER DDANWRKHSL AWIEGNDVKL AYRPVHLEPL TRQDEGGIDL KKIAPKARVY
//

If you have problems or comments...

PBIL Back to PBIL home page