(data stored in SCRATCH zone)

SWISSPROT: C5BDL7_EDWI9

ID   C5BDL7_EDWI9            Unreviewed;       599 AA.
AC   C5BDL7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=Fumarate reductase flavoprotein subunit {ECO:0000256|RuleBase:RU362050};
DE            EC=1.3.5.4 {ECO:0000256|RuleBase:RU362050};
GN   OrderedLocusNames=NT01EI_0392 {ECO:0000313|EMBL:ACR67633.2};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67633.2, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC       {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; CP001600; ACR67633.2; -; Genomic_DNA.
DR   RefSeq; WP_015869839.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0392; -.
DR   EnsemblBacteria; ACR67633; ACR67633; NT01EI_0392.
DR   GeneID; 7961220; -.
DR   KEGG; eic:NT01EI_0392; -.
DR   PATRIC; fig|634503.3.peg.356; -.
DR   eggNOG; ENOG4105C00; Bacteria.
DR   eggNOG; COG1053; LUCA.
DR   HOGENOM; HOG000160475; -.
DR   KO; K00244; -.
DR   OrthoDB; POG091H02TE; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:UniProtKB-UniRule.
DR   GO; GO:0009061; P:anaerobic respiration; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.58.100; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR005884; Fum_red_fp.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat.
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; 2.
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; C5BDL7.
DR   SWISS-2DPAGE; C5BDL7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
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:ACR67633.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
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}.
SQ   SEQUENCE   599 AA;  65975 MW;  87AF2C7BF8253E6E CRC64;
     MQTFNADLAI VGAGGAGLRA AIAAAEANPQ LKIALISKVY PMRSHTVAAE GGSAAVTQAH
     DSFDFHFHDT VAGGDWLCEQ DVVDHFVHNC PREMTQLELW GCPWSRKPDG SVNVRRFGGM
     KIERTWFAAD KTGFHMLHTL FQTSLKYPQI QRFDEHFVLD ILVDDGQARG VVAINMMEGT
     MVQIRANAVI LATGGAGRVY RYNTNGGIVT GDGMGMAFKH GIPLRDMEFV QYHPTGLPGS
     GILMTEGCRG EGGILVNKDG YRYLQDYGLG PETPLGEPKN KYMELGPRDK VSQAFWHEWR
     AGRTISTPRG DVVYLDLRHL GAKKLHERLP FICELAKAYV GVDPVNEPIP VRPTAHYTMG
     GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRVAGES ALQHLQNVTP
     TNGTALDAQV KDIEGNLKAL VNQEGNENWA TLRDEMGTSM EEGCGIYRTT DLMQKTVDKL
     AELKERFKHV KITDTSSVFN TELLYAIELE HGLNVAECMA HSAINRRESR GAHQRLDEGC
     TERDDVNFLK HTLTYFNESG APRIEYSDVK ITKLPPAKRV YGAEAEAQEA KKKEEKANG
//

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