Identification
Name:Succinate dehydrogenase hydrophobic membrane anchor subunit
Synonyms:Not Available
Gene Name:sdhD
Enzyme Class:Not Available
Biological Properties
General Function:Involved in succinate dehydrogenase activity
Specific Function:Membrane-anchoring subunit of succinate dehydrogenase (SDH)
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+AcceptorThumb+Reduced acceptor
Succinic acid + Acceptor ↔ Fumaric acid + Reduced acceptor
ReactionCard
SMPDB Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Ubiquinol 8+Thumb
Thumb+Coenzyme Q9Thumb+Thumb
Thumb+ThumbThumb+Ubiquinol-10+Thumb
Thumb+ThumbUbiquinol-0+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB00176Fumaric acidMetaboCard
ECMDB02434HydroquinoneMetaboCard
ECMDB23060QuinoneMetaboCard
ECMDB00254Succinic acidMetaboCard
ECMDB21574Ubiquinol-1MetaboCard
ECMDB20619Ubiquinol-10MetaboCard
ECMDB21575Ubiquinol-2MetaboCard
ECMDB21576Ubiquinol-3MetaboCard
ECMDB21577Ubiquinol-4MetaboCard
ECMDB21578Ubiquinol-5MetaboCard
ECMDB21460Ubiquinol-6MetaboCard
ECMDB21579Ubiquinol-7MetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21580Ubiquinol-9MetaboCard
ECMDB20487Ubiquinone-0MetaboCard
ECMDB21438Ubiquinone-1MetaboCard
ECMDB01072Ubiquinone-10MetaboCard
ECMDB21581Ubiquinone-2MetaboCard
ECMDB21582Ubiquinone-3MetaboCard
ECMDB23735Ubiquinone-4MetaboCard
ECMDB23734Ubiquinone-5MetaboCard
ECMDB20620Ubiquinone-6MetaboCard
ECMDB21584Ubiquinone-7MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane part
Function
binding
catalytic activity
cation binding
heme binding
ion binding
iron ion binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
succinate dehydrogenase activity
transition metal ion binding
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
tricarboxylic acid cycle
Gene Properties
Blattner:b0722
Gene OrientationClockwise
Centisome Percentage:16.27
Left Sequence End754783
Right Sequence End755130
Gene Sequence:
>348 bp
ATGGCTATCATCCCAAAAAACTATGCGCGGTTAGAAAGCGGCTATCGCGAAAAAGCATTA
AAAATCTATCCGTGGGTCTGCGGTCGCTGTTCCCGCGAGTTTGTTTATTCCAACCTGCGT
GAACTTACCGTTCACCACATTGATCACGACCATACCAATAACCCGGAAGATGGCAGTAAC
TGGGAATTGTTGTGTCTCTATTGCCACGATCATGAGCATTCGAAATATACCGAAGCGGAT
CAGTATGGTACGACCGTTATCGCAGGGGAAGATGCGCAGAAAGATGTCGGTGAAGCGAAG
TACAACCCATTCGCTGACCTGAAAGCGATGATGAACAAGAAGAAGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:115
Protein Molecular Weight:12867
Protein Theoretical pI:9
PDB File:1NEN
Signaling Regions:
  • None
Transmembrane Regions:
  • 16-36
  • 59-80
  • 91-115
Protein Sequence:
>Succinate dehydrogenase hydrophobic membrane anchor subunit
MVSNASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWIGFFASAFTKVF
TLLALFSILIHAWIGMWQVLTDYVKPLALRLMLQLVIVVALVVYVIYGFVVVWGV
References
External Links:
ResourceLink
Uniprot ID:P0AC44
Uniprot Name:DHSD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674550
PDB ID:1NEN
Ecogene ID:EG10934
Ecocyc:EG10934
ColiBase:b0722
Kegg Gene:b0722
EchoBASE ID:EB0927
CCDB:DHSD_ECOLI
BacMap:16128697
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Horsefield, R., Yankovskaya, V., Sexton, G., Whittingham, W., Shiomi, K., Omura, S., Byrne, B., Cecchini, G., Iwata, S. (2006). "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. Pubmed: 16407191
  • 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., Horiuchi, T., et, a. l. .. (1996). "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. Pubmed: 8905232
  • Ruprecht, J., Yankovskaya, V., Maklashina, E., Iwata, S., Cecchini, G. (2009). "Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site." J Biol Chem 284:29836-29846. Pubmed: 19710024
  • Vibat, C. R., Cecchini, G., Nakamura, K., Kita, K., Gennis, R. B. (1998). "Localization of histidine residues responsible for heme axial ligation in cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in Escherichia coli." Biochemistry 37:4148-4159. Pubmed: 9521736
  • Wood, D., Darlison, M. G., Wilde, R. J., Guest, J. R. (1984). "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli." Biochem J 222:519-534. Pubmed: 6383359
  • Yankovskaya, V., Horsefield, R., Tornroth, S., Luna-Chavez, C., Miyoshi, H., Leger, C., Byrne, B., Cecchini, G., Iwata, S. (2003). "Architecture of succinate dehydrogenase and reactive oxygen species generation." Science 299:700-704. Pubmed: 12560550