CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002427
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Succinate dehydrogenase iron-sulfur subunit 
Protein Synonyms/Alias
  
Gene Name
 sdhB 
Gene Synonyms/Alias
 b0724; JW0714 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
45ALIQLKEKDPSLSFRacetylation[1]
116QFYAQYEKIKPYLLNacetylation[1]
118YAQYEKIKPYLLNNGacetylation[1]
230TRAIGHIKSMLLQRNacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. 
Sequence Annotation
 DOMAIN 8 97 2Fe-2S ferredoxin-type.
 DOMAIN 139 169 4Fe-4S ferredoxin-type.
 METAL 55 55 Iron-sulfur 1 (2Fe-2S).
 METAL 60 60 Iron-sulfur 1 (2Fe-2S).
 METAL 75 75 Iron-sulfur 1 (2Fe-2S).
 METAL 149 149 Iron-sulfur 2 (4Fe-4S).
 METAL 152 152 Iron-sulfur 2 (4Fe-4S).
 METAL 155 155 Iron-sulfur 2 (4Fe-4S).
 METAL 159 159 Iron-sulfur 3 (3Fe-4S).
 METAL 206 206 Iron-sulfur 3 (3Fe-4S).
 METAL 212 212 Iron-sulfur 3 (3Fe-4S).
 METAL 216 216 Iron-sulfur 2 (4Fe-4S).
 BINDING 164 164 Ubiquinone; shared with SdhD subunit.  
Keyword
 2Fe-2S; 3D-structure; 3Fe-4S; 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Reference proteome; Transport; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 238 AA 
Protein Sequence
MRLEFSIYRY NPDVDDAPRM QDYTLEADEG RDMMLLDALI QLKEKDPSLS FRRSCREGVC 60
GSDGLNMNGK NGLACITPIS ALNQPGKKIV IRPLPGLPVI RDLVVDMGQF YAQYEKIKPY 120
LLNNGQNPPA REHLQMPEQR EKLDGLYECI LCACCSTSCP SFWWNPDKFI GPAGLLAAYR 180
FLIDSRDTET DSRLDGLSDA FSVFRCHSIM NCVSVCPKGL NPTRAIGHIK SMLLQRNA 238 
Gene Ontology
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IMP:EcoCyc.
 GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc.
 GO:0009055; F:electron carrier activity; IMP:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000104; F:succinate dehydrogenase activity; IEA:EC.
 GO:0009060; P:aerobic respiration; IEP:EcoCyc.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 
Interpro
 IPR001041; 2Fe-2S_ferredoxin-type.
 IPR017896; 4Fe4S_Fe-S-bd.
 IPR017900; 4Fe4S_Fe_S_CS.
 IPR012675; Beta-grasp_dom.
 IPR012285; Fum_reductase_C.
 IPR009051; Helical_ferredxn.
 IPR004489; Succ_DH/fum_Rdtase_Fe-S.
 IPR025192; Succ_DH/fum_Rdtase_N. 
Pfam
 PF13085; Fer2_3 
SMART
  
PROSITE
 PS00197; 2FE2S_FER_1
 PS51085; 2FE2S_FER_2
 PS00198; 4FE4S_FER_1
 PS51379; 4FE4S_FER_2 
PRINTS