(data stored in SCRATCH zone)

SWISSPROT: D3UZ99_XENBS

ID   D3UZ99_XENBS            Unreviewed;       598 AA.
AC   D3UZ99;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Fumarate reductase flavoprotein subunit {ECO:0000256|RuleBase:RU362050};
DE            EC=1.3.5.4 {ECO:0000256|RuleBase:RU362050};
GN   Name=frdA {ECO:0000313|EMBL:CBJ79681.1};
GN   OrderedLocusNames=XBJ1_0537 {ECO:0000313|EMBL:CBJ79681.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79681.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79681.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79681.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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=1.3.5.4;
CC         Evidence={ECO:0000256|RuleBase:RU362050};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362050};
CC   -!- SUBUNIT: Fumarate dehydrogenase forms part of an enzyme complex
CC       containing four subunits: a flavoprotein, an iron-sulfur, and two
CC       hydrophobic anchor proteins. {ECO:0000256|RuleBase:RU362050}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|RuleBase:RU362050}.
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DR   EMBL; FN667741; CBJ79681.1; -; Genomic_DNA.
DR   RefSeq; WP_012987137.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0537; -.
DR   EnsemblBacteria; CBJ79681; CBJ79681; XBJ1_0537.
DR   GeneID; 8830161; -.
DR   KEGG; xbo:XBJ1_0537; -.
DR   PATRIC; fig|406818.4.peg.492; -.
DR   eggNOG; ENOG4105C00; Bacteria.
DR   eggNOG; COG1053; LUCA.
DR   HOGENOM; HOG000160475; -.
DR   KO; K00244; -.
DR   OMA; AEGGYNA; -.
DR   BioCyc; XBOV406818:XBJ1_RS02335-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
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; IPR005884; Fum_red_fp.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
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; TIGR01176; fum_red_Fp; 1.
DR   TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UZ99.
DR   SWISS-2DPAGE; D3UZ99.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Electron transport {ECO:0000256|RuleBase:RU362050};
KW   FAD {ECO:0000256|RuleBase:RU362050};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362050};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362050,
KW   ECO:0000313|EMBL:CBJ79681.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transport {ECO:0000256|RuleBase:RU362050}.
FT   DOMAIN        7    397       FAD_binding_2. {ECO:0000259|Pfam:
FT                                PF00890}.
FT   DOMAIN      453    581       Succ_DH_flav_C. {ECO:0000259|Pfam:
FT                                PF02910}.
FT   COILED      423    443       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   598 AA;  66307 MW;  3FC32CB8690BEF81 CRC64;
     MQTFNADLAI IGAGGAGLRA AIAAAEANPQ LKIALISKVY PMRSHTVAAE GGSAAVTQSH
     DSYDFHFNDT VSGGDWLCEQ DVVEYFVKHC PTEMIQLEQW GCPWSRKEDG SVNVRRFGGM
     KIERTWFAAD KTGFHMLHTL FQTSLKYPQI QRFDEHFVLD ILVDEGQVRG LVALNMMEGT
     KVQIRANAVI MATGGAGRVY RYNTNGGIVT GDGMGMAFRH GIPLRDMEFV QYHPTGLPGS
     GILMTEGCRG EGGILVNKDG YRYLQDYGMG PETPLGQPEN KYMELGPRDK VSQAFWHEWQ
     AGRTIATPRG DVVHLDLRHL GEKKLLERLP FICELAKAYV GVDPVKEPIP VRPTAHYTMG
     GIETNPQCET RIKGLFAIGE CASVGLHGAN RLGSNSLAEL VVFGRLAGEE AVRHIQQTTP
     ANENALDAQA RDIENKLNKL LNQKGIESWA KIRDELGISM EEGCGIYRTP ELMQKTMDKI
     TELKERFRHI EITDRSSVFN TDLLYTIELG FGLDVAECMA HSAMNRKESR GAHQRLDAGC
     TERDDENFLK HTLAFYNPEG APRLEYSDVK ITISKPAKRV YGGEAAAQDK QQKEQANG
//

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