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UniProtKB/Swiss-Prot entry P21911


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

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Entry information
Entry name DHSB_SCHPO
Primary accession number P21911
Secondary accession number P21915
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on December 15, 1998 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 84)
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
ORFNames: SPAC140.01
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-228.
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).
[3]
ERRATUM.
Gould S.J., Subramani S., Scheffler I.E.;
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993).
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
CU329670; CAB86412.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D32394; D32394.
T37633; T37633.
RefSeq NP_593530.1; -.
3D structure databases
HSSP P07014; 1NEK. [HSSP ENTRY / PDB]
SMR P21911; 21-251.
ModBase P21911.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-001211-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC140.01; -.
Gene expression databases
ArrayExpress P21911; -.
Ontologies
GO
GO:0005743; Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
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:0008177; Molecular function: succinate dehydrogenase (ubiquinone) 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 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 P21911.
Genome annotation databases
GeneID 2542842; -.
KEGG spo:SPAC140.01; -.
NMPDR fig|4896.1.peg.3500; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; 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     ?        Mitochondrion. 
CHAIN   ?   252        Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial. PRO_0000010350
DOMAIN   34   114  81     2Fe-2S ferredoxin-type. 
DOMAIN   155   185  31     4Fe-4S ferredoxin-type. 
METAL   75    75        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   80    80        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   83    83        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   95    95        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   165   165        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   168   168        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   171   171        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   175   175        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   222   222        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   228   228        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   232   232        Iron-sulfur 2 (4Fe-4S) (By similarity). 
BINDING   180   180        Ubiquinone; shared with DHSD (By similarity). 
Sequence information
Length: 252 AA [This is the length of the unprocessed precursor] Molecular weight: 28595 Da [This is the MW of the unprocessed precursor] CRC64: 87A3DC0B3742DEE1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATEANISAT SANPQSQGEN LKTFEIYRWN PEKPEVKPKL QKYTVDLTKC GPMVLDALIK 

        70         80         90        100        110        120 
IKNEQDPTLT FRRSCREGIC GSCAMNINGS NTLACICNIK KDNKPTKIYP LPHCFIVKDL 

       130        140        150        160        170        180 
VPDLTYFYKQ YKSIEPWLQN DNIPKDKEFY QSRADRAKLD GLYECILCAC CSTSCPSYWW 

       190        200        210        220        230        240 
NSEEYLGPAV LMQAYRWIID SRDQATAKRL DVMQNSMSVY RCHTIMNCAR TCPKGLNPGL 

       250 
AIAKVKALMA TA 

P21911 in FASTA format

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