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UniProtKB/Swiss-Prot entry P00363


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FRDA_ECOLI
Primary accession number P00363
Secondary accession number Q2M6E8
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 105)
Name and origin of the protein
Protein name Fumarate reductase flavoprotein subunit
Synonym EC 1.3.99.1
Gene name
Name: frdA
OrderedLocusNames: b4154, JW4115
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=7037404 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T.;
"Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli.";
Eur. J. Biochem. 122:479-484(1982).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan]
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
MUTAGENESIS OF HIS-45.
PubMed=2668268 [NCBI, ExPASy, EBI, Israel, Japan]
Blaut M., Whittaker K., Valdovinos A., Ackrell B.A., Gunsalus R.P., Cecchini G.;
"Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin.";
J. Biol. Chem. 264:13599-13604(1989).
[6]
MUTAGENESIS OF HIS-233; CYS-248 AND ARG-249.
PubMed=1856194 [NCBI, ExPASy, EBI, Israel, Japan]
Schroeder I., Gunsalus R.P., Ackrell B.A.C., Cochran B., Cecchini G.;
"Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis.";
J. Biol. Chem. 266:13572-13579(1991).
[7]
MUTAGENESIS OF CYS-51.
DOI=10.1073/pnas.96.22.12412; PubMed=10535936 [NCBI, ExPASy, EBI, Israel, Japan]
Yi X., Mroczko M., Manoj K.M., Wang X., Hager L.P.;
"Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue.";
Proc. Natl. Acad. Sci. U.S.A. 96:12412-12417(1999).
[8]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
DOI=10.1126/science.284.5422.1961; PubMed=10373108 [NCBI, ExPASy, EBI, Israel, Japan]
Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C.;
"Structure of the Escherichia coli fumarate reductase respiratory complex.";
Science 284:1961-1966(1999).
[9]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
DOI=10.1074/jbc.M200815200; PubMed=11850430 [NCBI, ExPASy, EBI, Israel, Japan]
Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C.;
"Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.";
J. Biol. Chem. 277:16124-16130(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J01611; AAA23437.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97053.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77114.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78158.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00376; RDECFF.
RefSeq AP_004657.1; -.
NP_418578.1; -.
3D structure databases
PDB
1KF6; X-ray; 2.70 A; A/M=1-602.[ExPASy / RCSB / EBI]
1KFY; X-ray; 3.60 A; A/M=1-602.[ExPASy / RCSB / EBI]
1L0V; X-ray; 3.30 A; A/M=1-602.[ExPASy / RCSB / EBI]
2B76; X-ray; 3.30 A; A/M=1-602.[ExPASy / RCSB / EBI]
3CIR; X-ray; 3.65 A; A/M=1-602.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KF6; -.
1KFY; -.
1L0V; -.
2B76; -.
3CIR; -.
ModBase P00363.
Protein-protein interaction databases
DIP DIP:9681N; -.
IntAct P00363; -.
Enzyme and pathway databases
BioCyc EcoCyc:FUM-FLAVO; -.
MetaCyc:FUM-FLAVO; -.
2D gel databases
ECO2DBASE G063.2; 6TH EDITION.
Organism-specific databases
EchoBASE EB0326; -.
EcoGene EG10330; frdA.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR003953; FAD_bind2_N.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR003952; FRD_SDH_FAD_BS.
IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
IPR005884; Fum_red_fp.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR014006; Succ_Dhase_frdA_Gneg.
Graphical view of domain structure.
Pfam PF00890; FAD_binding_2; 1.
PF02910; Succ_DH_flav_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00411; PNDRDTASEI.
TIGRFAMs TIGR01176; fum_red_Fp; 1.
TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE PS00504; FRD_SDH_FAD_BINDING; 1.
BLOCKS P00363.
ProtoNet P00363.
Genome annotation databases
GeneID 948667; -.
GenomeReviews U00096_GR; b4154.
AP009048_GR; JW4115.
KEGG ecj:JW4115; -.
eco:b4154; -.
Phylogenomic databases
HOGENOM P00363; -.
Other
DrugBank DB00730; Thiabendazole.
LinkHub P00363; -.
Genome annotation databases
CMR P00363; b4154.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Electron transport; FAD; Flavoprotein; Oxidoreductase; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   602  601     Fumarate reductase flavoprotein subunit. PRO_0000158660
NP_BIND   9    23  15     FAD (Potential). 
ACT_SITE   233   233         
ACT_SITE   249   249         
MOD_RES   45    45        Tele-8alpha-FAD histidine. 
MUTAGEN   45    45        H->R: Inactivates enzyme. 
MUTAGEN   45    45        H->S,C,Y: Decreased ability (greater than 70%) to reduce fumarate. 
MUTAGEN   233   233        H->S: Severely affect succinate oxidation and decrease fumarate oxidation by 75%. 
MUTAGEN   248   248        C->S,A: Does not inactivate enzyme. 
MUTAGEN   249   249        R->H,L: Inactivates enzyme. 
CONFLICT   386   386        L -> P (in Ref. 1; AAA23437). 
STRAND   2     5  4      
STRAND   7    11  5      
HELIX   15    27  13      
STRAND   33    39  7      
HELIX   41    43  3      
HELIX   45    48  4      
HELIX   63    73  11      
TURN   74    76  3      
HELIX   80    99  20      
STRAND   110   112  3      
HELIX   132   144  13      
STRAND   150   154  5      
STRAND   156   164  9      
STRAND   167   175  9      
TURN   176   179  4      
STRAND   180   185  6      
STRAND   189   191  3      
HELIX   197   199  3      
STRAND   200   205  6      
HELIX   212   218  7      
TURN   219   221  3      
STRAND   224   226  3      
STRAND   230   236  7      
TURN   238   240  3      
HELIX   247   250  4      
STRAND   254   256  3      
HELIX   263   266  4      
TURN   267   269  3      
HELIX   283   285  3      
HELIX   288   301  14      
STRAND   312   316  5      
HELIX   318   320  3      
HELIX   322   328  7      
HELIX   330   340  11      
TURN   344   346  3      
STRAND   349   358  10      
STRAND   361   363  3      
STRAND   371   373  3      
STRAND   375   377  3      
HELIX   379   381  3      
STRAND   385   387  3      
HELIX   395   416  22      
HELIX   423   442  20      
HELIX   449   463  15      
STRAND   464   468  5      
HELIX   470   487  18      
HELIX   501   525  25      
TURN   545   547  3      
STRAND   550   556  7      
STRAND   562   568  7      
Sequence information
Length: 602 AA [This is the length of the unprocessed precursor] Molecular weight: 65972 Da [This is the MW of the unprocessed precursor] CRC64: 3306D7FF6E198AE9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQTFQADLAI VGAGGAGLRA AIAAAQANPN AKIALISKVY PMRSHTVAAE GGSAAVAQDH 

        70         80         90        100        110        120 
DSFEYHFHDT VAGGDWLCEQ DVVDYFVHHC PTEMTQLELW GCPWSRRPDG SVNVRRFGGM 

       130        140        150        160        170        180 
KIERTWFAAD KTGFHMLHTL FQTSLQFPQI QRFDEHFVLD ILVDDGHVRG LVAMNMMEGT 

       190        200        210        220        230        240 
LVQIRANAVV MATGGAGRVY RYNTNGGIVT GDGMGMALSH GVPLRDMEFV QYHPTGLPGS 

       250        260        270        280        290        300 
GILMTEGCRG EGGILVNKNG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR 

       310        320        330        340        350        360 
KGNTISTPRG DVVYLDLRHL GEKKLHERLP FICELAKAYV GVDPVKEPIP VRPTAHYTMG 

       370        380        390        400        410        420 
GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRLAGEQ ATERAATAGN 

       430        440        450        460        470        480 
GNEAAIEAQA AGVEQRLKDL VNQDGGENWA KIRDEMGLAM EEGCGIYRTP ELMQKTIDKL 

       490        500        510        520        530        540 
AELQERFKRV RITDTSSVFN TDLLYTIELG HGLNVAECMA HSAMARKESR GAHQRLDEGC 

       550        560        570        580        590        600 
TERDDVNFLK HTLAFRDADG TTRLEYSDVK ITTLPPAKRV YGGEADAADK AEAANKKEKA 


NG 

P00363 in FASTA format

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