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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
Galibert F.,
Alexandraki D.,
Baur A.,
Boles E.,
Chalwatzis N.,
Chuat J.-C.,
Coster F.,
Cziepluch C.,
de Haan M.,
Domdey H.,
Durand P.,
Entian K.-D.,
Gatius M.,
Goffeau A.,
Grivell L.A.,
Hennemann A.,
Herbert C.J.,
Heumann K.,
Hilger F.,
Hollenberg C.P.,
Huang M.-E.,
Jacq C.,
Jauniaux J.-C.,
Katsoulou C.,
Kirchrath L.,
Kleine K.,
Kordes E.,
Koetter P.,
Liebl S.,
Louis E.J.,
Manus V.,
Mewes H.-W.,
Miosga T.,
Obermaier B.,
Perea J.,
Pohl T.M.,
Portetelle D.,
Pujol A.,
Purnelle B.,
Ramezani Rad M.,
Rasmussen S.W.,
Rose M.,
Rossau R.,
Schaaff-Gerstenschlaeger I.,
Smits P.H.M.,
Scarcez T.,
Soriano N.,
To Van D.,
Tzermia M.,
Van Broekhoven A.,
Vandenbol M.,
Wedler H.,
von Wettstein D.,
Wambutt R.,
Zagulski M.,
Zollner A.,
Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
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[2]
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FUNCTION.
DOI=10.1002/(SICI)1097-0061(199808)14:11<1001::AID-YEA304>3.0.CO;2-K; PubMed=9730279 [NCBI, ExPASy, EBI, Israel, Japan]
Colby G.,
Ishii Y.,
Tzagoloff A.;
"Suppression of sdh1 mutations by the SDH1b gene of Saccharomyces cerevisiae.";
Yeast 14:1001-1006(1998).
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- FUNCTION: Probable minor catalytic subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Probably forms a catalytic dimer with SDH2. Electrons flow from succinate to the FAD bound to the catalytic subunit, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
- CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol.
- COFACTOR: FAD.
- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
- SUBUNIT: Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit (By similarity).
- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
- MISCELLANEOUS: In vitro, can complement a SDH1 disruption and leads to less than 15% of wild-type SDH reductase activity probably due to its lower expression level (compared to SDH1).
- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 634 AA [This is the length of the unprocessed precursor] |
Molecular weight: 69382 Da [This is the MW of the unprocessed precursor] |
CRC64: F00CD157AB9BF9C5 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MLSLKKGITK SYILQRTFTS SSVVRQIGEV KSESKPPAKY HIIDHEYDCV VVGAGGAGLR
70 80 90 100 110 120
AAFGLAEAGY KTACLSKLFP TRSHTVAAQG GINAALGNMH PDDWKSHMYD TVKGSDWLGD
130 140 150 160 170 180
QDAIHYMTRE APKSVIELEH YGMPFSRTED GRIYQRAFGG QSKDFGKGGQ AYRTCAVADR
190 200 210 220 230 240
TGHAMLHTLY GQALKNNTHF FIEYFAMDLL THNGEVVGVI AYNQEDGTIH RFRAHKTVIA
250 260 270 280 290 300
TGGYGRAYFS CTSAHTCTGD GNAMVSRAGF PLEDLEFVQF HPSGIYGSGC LITEGARGEG
310 320 330 340 350 360
GFLLNSEGER FMERYAPTAK DLASRDVVSR AITMEIRAGR GVGKNKDHIL LQLSHLPPEV
370 380 390 400 410 420
LKERLPGISE TAAVFAGVDV TQEPIPVLPT VHYNMGGIPT KWTGEALTID EETGEDKVIP
430 440 450 460 470 480
GLMACGEAAC VSVHGANRLG ANSLLDLVVF GRAVANTIAD TLQPGLPHKP LASNIGHESI
490 500 510 520 530 540
ANLDKVRNAR GSLKTSQIRL NMQRTMQKDV SVFRTQDTLD EGVRNITEVD KTFEDVHVSD
550 560 570 580 590 600
KSMIWNSDLV ETLELQNLLT CATQTAVSAS KRKESRGAHA REDYAKRDDV NWRKHTLSWQ
610 620 630
KGTSTPVKIK YRNVIAHTLD ENECAPVPPA VRSY
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P47052 in FASTA format |
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