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UniProtKB/Swiss-Prot entry P0AC41


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

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Entry information
Entry name DHSA_ECOLI
Primary accession number P0AC41
Secondary accession numbers P10444 P78282
Integrated into Swiss-Prot on November 8, 2005
Sequence was last modified on November 8, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 37)
Name and origin of the protein
Protein name Succinate dehydrogenase flavoprotein subunit
Synonym EC 1.3.99.1
Gene name
Name: sdhA
OrderedLocusNames: b0723, JW0713
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=6383359 [NCBI, ExPASy, EBI, Israel, Japan]
Wood D., Darlison M.G., Wilde R.J., Guest J.R.;
"Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli.";
Biochem. J. 222:519-534(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[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 578-588.
STRAIN=K12;
PubMed=6388571 [NCBI, ExPASy, EBI, Israel, Japan]
Darlison M.G., Guest J.R.;
"Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli.";
Biochem. J. 223:507-517(1984).
[6]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[7]
PROTEIN SEQUENCE OF 1-4.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1006/jmbi.1998.1726; PubMed=9600841 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[8]
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
DOI=10.1074/jbc.M506479200; PubMed=16079137 [NCBI, ExPASy, EBI, Israel, Japan]
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
[10]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, ENZYME REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
DOI=10.1126/science.1079605; PubMed=12560550 [NCBI, ExPASy, EBI, Israel, Japan]
Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C., Miyoshi H., Leger C., Byrne B., Cecchini G., Iwata S.;
"Architecture of succinate dehydrogenase and reactive oxygen species generation.";
Science 299:700-704(2003).
[11]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, AND SUBUNIT.
DOI=10.1074/jbc.M508173200; PubMed=16407191 [NCBI, ExPASy, EBI, Israel, Japan]
Horsefield R., Yankovskaya V., Sexton G., Whittingham W., Shiomi K., Omura S., Byrne B., Cecchini G., Iwata S.;
"Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction.";
J. Biol. Chem. 281:7309-7316(2006).
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
J01619; AAA23895.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00980; CAA25487.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73817.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35390.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01070; CAA25533.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B64808; DEECSF.
RefSeq AP_001361.1; -.
NP_415251.1; -.
3D structure databases
PDB
1NEK; X-ray; 2.60 A; A=1-588.[ExPASy / RCSB / EBI]
1NEN; X-ray; 2.90 A; A=1-588.[ExPASy / RCSB / EBI]
2ACZ; X-ray; 3.10 A; A=1-588.[ExPASy / RCSB / EBI]
2AD0; Model; -; A=1-588.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NEK; -.
1NEN; -.
2ACZ; -.
2AD0; -.
ModBase P0AC41.
Protein-protein interaction databases
IntAct P0AC41; 90.
Enzyme and pathway databases
BioCyc EcoCyc:SDH-FLAVO; -.
MetaCyc:SDH-FLAVO; -.
2D gel databases
SWISS-2DPAGE P0AC41; -.
ECO2DBASE F060.3; 6TH EDITION.
Organism-specific databases
EchoBASE EB0924; -.
EcoGene EG10931; sdhA.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000104; Molecular function: succinate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
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.
IPR011281; Succ_DHase_flav_su_fwd.
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.
TIGRFAMs TIGR01816; sdhA_forward; 1.
TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE PS00504; FRD_SDH_FAD_BINDING; 1.
Genome annotation databases
GeneID 945402; -.
GenomeReviews AP009048_GR; JW0713.
U00096_GR; b0723.
KEGG ecj:JW0713; -.
eco:b0723; -.
Phylogenomic databases
HOGENOM P0AC41; -.
Genome annotation databases
CMR P0AC41; b0723.
Other
ProtoNet P0AC41.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; Oxidoreductase; Transport; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   588  588     Succinate dehydrogenase flavoprotein subunit. PRO_0000158652
NP_BIND   37    52  16     FAD. 
ACT_SITE   286   286        Proton acceptor. 
BINDING   242   242        Substrate. 
BINDING   254   254        Substrate. 
BINDING   354   354        Substrate. 
BINDING   399   399        Substrate. 
MOD_RES   45    45        Tele-8alpha-FAD histidine. 
MOD_RES   267   267        N6-acetyllysine. 
CONFLICT   20    22        MRA -> IAR (in Ref. 1; AAA23895/CAA25487). 
STRAND   5     9  5      
STRAND   11    13  3      
HELIX   17    28  12      
STRAND   34    36  3      
HELIX   41    43  3      
HELIX   45    48  4      
STRAND   59    61  3      
HELIX   65    76  12      
HELIX   82   101  20      
STRAND   119   121  3      
STRAND   123   125  3      
STRAND   129   135  7      
HELIX   141   155  15      
STRAND   159   161  3      
STRAND   163   171  9      
STRAND   177   184  8      
TURN   185   187  3      
STRAND   190   196  7      
STRAND   198   200  3      
HELIX   206   208  3      
STRAND   209   214  6      
HELIX   221   227  7      
TURN   228   230  3      
STRAND   233   235  3      
STRAND   239   246  8      
TURN   247   249  3      
HELIX   256   260  5      
STRAND   263   265  3      
HELIX   272   276  5      
TURN   278   280  3      
HELIX   281   283  3      
HELIX   286   298  13      
STRAND   305   307  3      
STRAND   309   314  6      
HELIX   320   326  7      
HELIX   328   338  11      
TURN   342   344  3      
STRAND   347   356  10      
STRAND   359   362  4      
STRAND   367   371  5      
STRAND   373   375  3      
STRAND   377   385  9      
STRAND   387   391  5      
STRAND   393   395  3      
HELIX   403   426  24      
HELIX   434   440  7      
HELIX   442   449  8      
STRAND   452   454  3      
HELIX   456   470  15      
STRAND   472   475  4      
HELIX   477   493  17      
HELIX   494   496  3      
HELIX   508   532  25      
STRAND   541   545  5      
TURN   550   552  3      
STRAND   558   560  3      
STRAND   568   570  3      
Sequence information
Length: 588 AA [This is the length of the unprocessed precursor] Molecular weight: 64422 Da [This is the MW of the unprocessed precursor] CRC64: 837F9A63991B6CE8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ GGITVALGNT 

        70         80         90        100        110        120 
HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE HMGLPFSRLD DGRIYQRPFG 

       130        140        150        160        170        180 
GQSKNFGGEQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAVVGC 

       190        200        210        220        230        240 
TALCIETGEV VYFKARATVL ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ 

       250        260        270        280        290        300 
FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG 

       310        320        330        340        350        360 
RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI PTCHYMMGGI 

       370        380        390        400        410        420 
PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL GGNSLLDLVV FGRAAGLHLQ 

       430        440        450        460        470        480 
ESIAEQGALR DASESDVEAS LDRLNRWNNN RNGEDPVAIR KALQECMQHN FSVFREGDAM 

       490        500        510        520        530        540 
AKGLEQLKVI RERLKNARLD DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH 

       550        560        570        580 
SRFDFPDRDD ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY 

P0AC41 in FASTA format

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