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Protein

Succinate dehydrogenase iron-sulfur subunit

Gene

sdhB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551Iron-sulfur 1 (2Fe-2S)
Metal bindingi60 – 601Iron-sulfur 1 (2Fe-2S)
Metal bindingi75 – 751Iron-sulfur 1 (2Fe-2S)
Metal bindingi149 – 1491Iron-sulfur 2 (4Fe-4S)
Metal bindingi152 – 1521Iron-sulfur 2 (4Fe-4S)
Metal bindingi155 – 1551Iron-sulfur 2 (4Fe-4S)
Metal bindingi159 – 1591Iron-sulfur 3 (3Fe-4S)
Binding sitei164 – 1641Ubiquinone; shared with SdhD subunit1 Publication
Metal bindingi206 – 2061Iron-sulfur 3 (3Fe-4S)
Metal bindingi212 – 2121Iron-sulfur 3 (3Fe-4S)
Metal bindingi216 – 2161Iron-sulfur 2 (4Fe-4S)

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: EcoCyc
  2. 3 iron, 4 sulfur cluster binding Source: EcoCyc
  3. 4 iron, 4 sulfur cluster binding Source: EcoCyc
  4. electron carrier activity Source: EcoCyc
  5. iron-sulfur cluster binding Source: EcoCyc
  6. metal ion binding Source: UniProtKB-KW
  7. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

GO - Biological processi

  1. aerobic respiration Source: EcoCyc
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:SDH-FE-S.
ECOL316407:JW0714-MONOMER.
MetaCyc:SDH-FE-S.
UniPathwayiUPA00223; UER01005.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase iron-sulfur subunit (EC:1.3.5.1)
Gene namesi
Name:sdhB
Ordered Locus Names:b0724, JW0714
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10932. sdhB.

Subcellular locationi

Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Succinate dehydrogenase iron-sulfur subunitPRO_0000158688Add
BLAST

Proteomic databases

PaxDbiP07014.
PRIDEiP07014.

Expressioni

Gene expression databases

GenevestigatoriP07014.

Interactioni

Subunit structurei

Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic anchor protein. The complex forms trimers.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
sdhAP0AC412EBI-1035514,EBI-371263

Protein-protein interaction databases

BioGridi849677. 1 interaction.
DIPiDIP-10836N.
IntActiP07014. 8 interactions.
STRINGi511145.b0724.

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Turni12 – 143Combined sources
Beta strandi19 – 268Combined sources
Beta strandi29 – 313Combined sources
Helixi35 – 4511Combined sources
Beta strandi54 – 607Combined sources
Beta strandi64 – 674Combined sources
Beta strandi70 – 734Combined sources
Helixi74 – 763Combined sources
Helixi79 – 813Combined sources
Beta strandi89 – 924Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi103 – 1053Combined sources
Helixi108 – 1169Combined sources
Beta strandi130 – 1323Combined sources
Helixi137 – 1415Combined sources
Turni142 – 1487Combined sources
Helixi156 – 1583Combined sources
Helixi160 – 1645Combined sources
Turni166 – 1683Combined sources
Helixi172 – 18211Combined sources
Helixi190 – 1956Combined sources
Turni200 – 2056Combined sources
Helixi211 – 2155Combined sources
Helixi222 – 23716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NEKX-ray2.60B1-238[»]
1NENX-ray2.90B1-238[»]
2ACZX-ray3.10B1-238[»]
2AD0model-B1-238[»]
2WDQX-ray2.40B/F/J1-238[»]
2WDRX-ray3.20B/F/J1-238[»]
2WDVX-ray3.20B/F/J1-238[»]
2WP9X-ray2.70B/F/J1-238[»]
2WS3X-ray3.20B/F/J1-238[»]
2WU2X-ray2.50B/F/J1-238[»]
2WU5X-ray2.80B/F/J1-238[»]
ProteinModelPortaliP07014.
SMRiP07014. Positions 1-238.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07014.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 97902Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini139 – 169314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
InParanoidiP07014.
KOiK00240.
OMAiDMEPFFQ.
OrthoDBiEOG6CK7MG.
PhylomeDBiP07014.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07014-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLEFSIYRY NPDVDDAPRM QDYTLEADEG RDMMLLDALI QLKEKDPSLS
60 70 80 90 100
FRRSCREGVC GSDGLNMNGK NGLACITPIS ALNQPGKKIV IRPLPGLPVI
110 120 130 140 150
RDLVVDMGQF YAQYEKIKPY LLNNGQNPPA REHLQMPEQR EKLDGLYECI
160 170 180 190 200
LCACCSTSCP SFWWNPDKFI GPAGLLAAYR FLIDSRDTET DSRLDGLSDA
210 220 230
FSVFRCHSIM NCVSVCPKGL NPTRAIGHIK SMLLQRNA
Length:238
Mass (Da):26,770
Last modified:April 1, 1988 - v1
Checksum:i226F60C55F5AC35A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23896.1.
X01070 Genomic DNA. Translation: CAA25534.1.
U00096 Genomic DNA. Translation: AAC73818.1.
AP009048 Genomic DNA. Translation: BAA35391.1.
X00661 Genomic DNA. Translation: CAA25279.1.
PIRiA28837. DEECSI.
RefSeqiNP_415252.1. NC_000913.3.
YP_489004.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73818; AAC73818; b0724.
BAA35391; BAA35391; BAA35391.
GeneIDi12932956.
945300.
KEGGiecj:Y75_p0704.
eco:b0724.
PATRICi32116643. VBIEscCol129921_0754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23896.1.
X01070 Genomic DNA. Translation: CAA25534.1.
U00096 Genomic DNA. Translation: AAC73818.1.
AP009048 Genomic DNA. Translation: BAA35391.1.
X00661 Genomic DNA. Translation: CAA25279.1.
PIRiA28837. DEECSI.
RefSeqiNP_415252.1. NC_000913.3.
YP_489004.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NEKX-ray2.60B1-238[»]
1NENX-ray2.90B1-238[»]
2ACZX-ray3.10B1-238[»]
2AD0model-B1-238[»]
2WDQX-ray2.40B/F/J1-238[»]
2WDRX-ray3.20B/F/J1-238[»]
2WDVX-ray3.20B/F/J1-238[»]
2WP9X-ray2.70B/F/J1-238[»]
2WS3X-ray3.20B/F/J1-238[»]
2WU2X-ray2.50B/F/J1-238[»]
2WU5X-ray2.80B/F/J1-238[»]
ProteinModelPortaliP07014.
SMRiP07014. Positions 1-238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi849677. 1 interaction.
DIPiDIP-10836N.
IntActiP07014. 8 interactions.
STRINGi511145.b0724.

Proteomic databases

PaxDbiP07014.
PRIDEiP07014.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73818; AAC73818; b0724.
BAA35391; BAA35391; BAA35391.
GeneIDi12932956.
945300.
KEGGiecj:Y75_p0704.
eco:b0724.
PATRICi32116643. VBIEscCol129921_0754.

Organism-specific databases

EchoBASEiEB0925.
EcoGeneiEG10932. sdhB.

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
InParanoidiP07014.
KOiK00240.
OMAiDMEPFFQ.
OrthoDBiEOG6CK7MG.
PhylomeDBiP07014.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01005.
BioCyciEcoCyc:SDH-FE-S.
ECOL316407:JW0714-MONOMER.
MetaCyc:SDH-FE-S.

Miscellaneous databases

EvolutionaryTraceiP07014.
PROiP07014.

Gene expression databases

GenevestigatoriP07014.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli."
    Darlison M.G., Guest J.R.
    Biochem. J. 223:507-517(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12."
    Darlison M.G., Spencer M.E., Guest J.R.
    Eur. J. Biochem. 141:351-359(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-238.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / EMG2.
  7. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  8. "Architecture of succinate dehydrogenase and reactive oxygen species generation."
    Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C., Miyoshi H., Leger C., Byrne B., Cecchini G., Iwata S.
    Science 299:700-704(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTERS AND UBIQUINONE, COFACTOR, SUBUNIT.
  9. "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."
    Horsefield R., Yankovskaya V., Sexton G., Whittingham W., Shiomi K., Omura S., Byrne B., Cecchini G., Iwata S.
    J. Biol. Chem. 281:7309-7316(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTERS, COFACTOR, SUBUNIT.
  10. "Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site."
    Ruprecht J., Yankovskaya V., Maklashina E., Iwata S., Cecchini G.
    J. Biol. Chem. 284:29836-29846(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTERS, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiSDHB_ECOLI
AccessioniPrimary (citable) accession number: P07014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: January 7, 2015
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.