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UniProtKB/Swiss-Prot entry P21801


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

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Entry information
Entry name DHSB_YEAST
Primary accession number P21801
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on May 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial [Precursor]
Synonyms EC 1.3.5.1
Iron-sulfur subunit of complex II
Ip
Gene name
Name: SDH2
Synonyms: SDH, SDHB
OrderedLocusNames: YLL041C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2191948 [NCBI, ExPASy, EBI, Israel, Japan]
Lombardo A., Carine K., Scheffler I.E.;
"Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae.";
J. Biol. Chem. 265:10419-10423(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-242.
PubMed=2494655 [NCBI, ExPASy, EBI, Israel, Japan]
Gould S.J., Subramani S., Scheffler I.E.;
"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species.";
Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989).
[5]
ERRATUM.
Gould S.J., Subramani S., Scheffler I.E.;
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993).
[6]
MUTAGENESIS OF LYS-260; LYS-261 AND 260-LYS--ALA-266.
DOI=10.1021/bi00151a008; PubMed=1390628 [NCBI, ExPASy, EBI, Israel, Japan]
Schmidt D.M., Saghbini M., Scheffler I.E.;
"The C-terminus of the succinate dehydrogenase IP peptide of Saccharomyces cerevisiae is significant for assembly of complex II.";
Biochemistry 31:8442-8448(1992).
[7]
REVIEW ON SUCCINATE DEHYDROGENASE.
DOI=10.1016/S0005-2728(01)00229-8; PubMed=11803020 [NCBI, ExPASy, EBI, Israel, Japan]
Lemire B.D., Oyedotun K.S.;
"The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase.";
Biochim. Biophys. Acta 1553:102-116(2002).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
3D-STRUCTURE MODELING OF 21-266.
DOI=10.1074/jbc.M311876200; PubMed=14672929 [NCBI, ExPASy, EBI, Israel, Japan]
Oyedotun K.S., Lemire B.D.;
"The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies.";
J. Biol. Chem. 279:9424-9431(2004).
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
J05487; AAA35021.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73146; CAA97492.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558189; AAS56515.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35435; RDBYIS.
RefSeq NP_013059.1; -.
3D structure databases
PDB
1ORZ; Model; -; B=21-266.[ExPASy / RCSB / EBI]
1PB4; Model; -; B=21-266.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ORZ; -.
1PB4; -.
SMR P21801; 30-264.
ModBase P21801.
Protein-protein interaction databases
DIP DIP:5856N; -.
IntAct P21801; -.
Organism-specific databases
CYGD YLL041c; -.
SGD S000003964; SDH2.
Yeast-GFP YLL041C.
Gene expression databases
GermOnline YLL041C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005749; Cellular component: mitochondrial respiratory chain complex II (traceable author statement from SGD).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051538; Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008177; Molecular function: succinate dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0006121; Biological process: mitochondrial electron transport, succinate to ubiquinone (traceable author statement from SGD).
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 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.
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).
ProtoNet P21801.
Proteomic databases
PeptideAtlas P21801; -.
Genome annotation databases
Ensembl YLL041C; Saccharomyces cerevisiae. [Contig view]
GeneID 850685; -.
GenomeReviews Y13138_GR; YLL041C.
KEGG sce:YLL041C; -.
NMPDR fig|4932.3.peg.4050; -.
Phylogenomic databases
HOGENOM P21801; -.
Other
LinkHub P21801; -.
NextBio 966692; -.
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; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1   ?20        Mitochondrion. 
CHAIN   ?21   266        Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial. PRO_0000010353
DOMAIN   36   127  92     2Fe-2S ferredoxin-type. 
DOMAIN   169   199  31     4Fe-4S ferredoxin-type. 
METAL   87    87        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   92    92        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   95    95        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   107   107        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   179   179        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   182   182        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   185   185        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   189   189        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   236   236        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   242   242        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   246   246        Iron-sulfur 2 (4Fe-4S) (By similarity). 
BINDING   194   194        Ubiquinone; shared with DHSD (By similarity). 
MUTAGEN   260   266        Missing: Abolishes SDH activity and complex assembly. 
MUTAGEN   260   260        K->T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-261. 
MUTAGEN   261   261        K->T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-260. 
STRAND   32    39  8      
STRAND   43    45  3      
STRAND   47    49  3      
STRAND   52    58  7      
HELIX   66    75  10      
STRAND   87    90  4      
STRAND   96   102  7      
TURN   106   108  3      
STRAND   120   122  3      
STRAND   125   131  7      
HELIX   138   146  9      
STRAND   160   162  3      
HELIX   167   171  5      
TURN   172   178  7      
HELIX   184   187  4      
HELIX   190   194  5      
TURN   195   198  4      
HELIX   202   213  12      
HELIX   220   227  8      
TURN   230   235  6      
HELIX   241   245  5      
HELIX   252   265  14      
Sequence information
Length: 266 AA [This is the length of the unprocessed precursor] Molecular weight: 30231 Da [This is the MW of the unprocessed precursor] CRC64: C14170F3670F6930 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLNVLLRRKA FCLVTKKGMA TATTAAATHT PRLKTFKVYR WNPDEPSAKP HLQSYQVDLN 

        70         80         90        100        110        120 
DCGPMVLDAL LKIKDEQDST LTFRRSCREG ICGSCAMNIG GRNTLACICK IDQNESKQLK 

       130        140        150        160        170        180 
IYPLPHMFIV KDLVPDLTNF YQQYKSIQPY LQRSSFPKDG TEVLQSIEDR KKLDGLYECI 

       190        200        210        220        230        240 
LCACCSTSCP SYWWNQEQYL GPAVLMQAYR WLIDSRDQAT KTRKAMLNNS MSLYRCHTIM 

       250        260 
NCTRTCPKGL NPGLAIAEIK KSLAFA 

P21801 in FASTA format

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