(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NT12_YERPA

ID   A0A0E1NT12_YERPA        Unreviewed;       588 AA.
AC   A0A0E1NT12;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 24.
DE   RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|RuleBase:RU362051};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN   OrderedLocusNames=YPA_0589 {ECO:0000313|EMBL:ABG12557.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12557.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12557.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12557.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12557.1; -; Genomic_DNA.
DR   RefSeq; WP_002210724.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12557; ABG12557; YPA_0589.
DR   EnsemblBacteria; AJJ80001; AJJ80001; CH58_3447.
DR   KEGG; ypa:YPA_0589; -.
DR   PATRIC; fig|360102.15.peg.3615; -.
DR   KO; K00239; -.
DR   OMA; GDSPWEH; -.
DR   UniPathway; UPA00223; UER01005.
DR   Proteomes; UP000001971; 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; A0A0E1NT12.
DR   SWISS-2DPAGE; A0A0E1NT12.
KW   Cell inner membrane {ECO:0000256|RuleBase:RU362051};
KW   Cell membrane {ECO:0000256|RuleBase:RU362051};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
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:ABG12557.1};
KW   Transport {ECO:0000256|RuleBase:RU362051};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
SQ   SEQUENCE   588 AA;  64305 MW;  E6CE1AD417F77D88 CRC64;
     MNLPIREFDA VVVGAGGAGM RAALQISQMG LSCALISKVF PTRSHTVSAQ GGITVALGNT
     HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAVLELE HMGLPFSRLE DGSIYQRPFG
     GQSLNFGGGQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAFVGC
     TAINIETGEV VYFKARATIL ATGGAGRIYQ STTNAHINTG DGVGMALRAG VPVQDMEMWQ
     FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG
     RGCDGPWGPH AKLKLDHLGK DVLESRLPGI LELSRTFAHV DPIKEPIPVI PTCHYMMGGI
     PTKVTGQAIT VNEKGEDVVI PGLFAVGEIA CVSVHGANRL GGNSLLDLVV FGRAAGMHLQ
     ESLMEQGASR DASESDIEAS LARMNRWNNT RSGEDPVEIR KALQACMQNN FSVFREGDAM
     AKGLEELKTI RERLQNARLD DTSSEFNTQR IECLELDNLM ETAFSTAVSA NFRTESRGAH
     SRFDFPDRDD VNWLCHSLYL PGTESMTRRE VNMQPKLREA FPPKVRSY
//

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