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UniProtKB/Swiss-Prot entry P0AC47


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

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Entry information
Entry name FRDB_ECOLI
Primary accession number P0AC47
Secondary accession numbers P00364 Q2M6E9
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 30)
Name and origin of the protein
Protein name Fumarate reductase iron-sulfur subunit
Synonym EC 1.3.99.1
Gene name
Name: frdB
OrderedLocusNames: b4153, JW4114
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=6751816 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T., Grundstroem T., Jaurin B., Robinson J.J., Weiner J.H.;
"Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli.";
Eur. J. Biochem. 126:211-216(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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-244.
PubMed=7041115 [NCBI, ExPASy, EBI, Israel, Japan]
Grundstroem T., Jaurin B.;
"Overlap between ampC and frd operons on the Escherichia coli chromosome.";
Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982).
[6]
MUTAGENESIS.
PubMed=2174169 [NCBI, ExPASy, EBI, Israel, Japan]
Werth M.T., Cecchini G., Manodori A., Ackrell B.A.C., Schroeder I., Gunsalus R.P., Johnson M.K.;
"Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster.";
Proc. Natl. Acad. Sci. U.S.A. 87:8965-8969(1990).
[7]
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).
[8]
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; AAA23438.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97052.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77113.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78157.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00277; CAA23534.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00377; RDECFS.
RefSeq AP_004656.1; -.
NP_418577.1; -.
3D structure databases
PDB
1KF6; X-ray; 2.70 A; B/N=1-244.[ExPASy / RCSB / EBI]
1KFY; X-ray; 3.60 A; B/N=1-244.[ExPASy / RCSB / EBI]
1L0V; X-ray; 3.30 A; B/N=1-244.[ExPASy / RCSB / EBI]
2B76; X-ray; 3.30 A; B/N=1-244.[ExPASy / RCSB / EBI]
3CIR; X-ray; 3.65 A; B/N=2-244.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KF6; -.
1KFY; -.
1L0V; -.
2B76; -.
3CIR; -.
ModBase P0AC47.
Protein-protein interaction databases
IntAct P0AC47; -.
Enzyme and pathway databases
BioCyc EcoCyc:FUM-FE-S; -.
MetaCyc:FUM-FE-S; -.
2D gel databases
ECO2DBASE H024.7; 6TH EDITION.
Organism-specific databases
EchoBASE EB0327; -.
EcoGene EG10331; frdB.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR006058; 2Fe2S_fd_BS.
IPR001450; 4Fe4S_Fe_S_bd.
IPR012675; b-grasp_ferredoxin-like.
IPR001041; Ferredoxin.
IPR012285; Fum_reductase_C.
IPR004489; Succ_DHase/fum_Rdtase_Fe-S.
Graphical view of domain structure.
Gene3D G3DSA:3.10.20.30; Ferredoxin_fold; 1.
G3DSA:1.10.1060.10; Fum_reductase_C; 1.
Pfam PF00111; Fer2; 1.
PF00037; Fer4; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00384; dhsB; 1.
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS00198; 4FE4S_FER_1; 1.
PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P0AC47.
Genome annotation databases
GeneID 948666; -.
GenomeReviews U00096_GR; b4153.
AP009048_GR; JW4114.
KEGG ecj:JW4114; -.
eco:b4153; -.
Phylogenomic databases
HOGENOM P0AC47; -.
Other
LinkHub P0AC47; -.
Genome annotation databases
CMR P0AC47; b4153.
Other
ProtoNet P0AC47.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; 3D-structure; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Transport; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   244  243     Fumarate reductase iron-sulfur subunit. PRO_0000158698
DOMAIN   16    97  82     2Fe-2S ferredoxin-type. 
DOMAIN   140   169  30     4Fe-4S ferredoxin-type. 
METAL   58    58        Iron-sulfur 1 (2Fe-2S). 
METAL   63    63        Iron-sulfur 1 (2Fe-2S). 
METAL   66    66        Iron-sulfur 1 (2Fe-2S). 
METAL   78    78        Iron-sulfur 1 (2Fe-2S). 
METAL   149   149        Iron-sulfur 2 (4Fe-4S). 
METAL   152   152        Iron-sulfur 2 (4Fe-4S). 
METAL   155   155        Iron-sulfur 2 (4Fe-4S). 
METAL   159   159        Iron-sulfur 3 (3Fe-4S). 
METAL   205   205        Iron-sulfur 3 (3Fe-4S). 
METAL   211   211        Iron-sulfur 3 (3Fe-4S). 
METAL   215   215        Iron-sulfur 2 (4Fe-4S). 
MUTAGEN   58    58        C->S: Affects center 1 (2Fe-2S). 
MUTAGEN   63    63        C->S: Affects center 1 (2Fe-2S). 
MUTAGEN   66    66        C->S: Affects center 1 (2Fe-2S). 
MUTAGEN   78    78        C->S: Affects center 1 (2Fe-2S). 
STRAND   5    13  9      
TURN   16    18  3      
STRAND   23    31  9      
HELIX   37    47  11      
STRAND   59    63  5      
STRAND   67    70  4      
STRAND   73    76  4      
HELIX   77    79  3      
HELIX   82    84  3      
STRAND   89    93  5      
STRAND   99   101  3      
HELIX   108   116  9      
HELIX   128   130  3      
HELIX   137   141  5      
HELIX   144   147  4      
HELIX   154   158  5      
HELIX   160   164  5      
HELIX   171   181  11      
HELIX   190   197  8      
TURN   199   201  3      
HELIX   202   204  3      
HELIX   210   214  5      
HELIX   221   240  20      
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 27123 Da [This is the MW of the unprocessed precursor] CRC64: AC1D7A73244D7AC0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM 

        70         80         90        100        110        120 
AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY 

       130        140        150        160        170        180 
IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY 

       190        200        210        220        230        240 
NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT 


LKPR 

P0AC47 in FASTA format

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