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P0AC41 (SDHA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate dehydrogenase flavoprotein subunit

EC=1.3.5.1
Gene names
Name:sdhA
Ordered Locus Names:b0723, JW0713
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

FAD. Ref.13

Enzyme regulation

Inhibited by oxaloacetate. Ref.11

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.

Subunit structure

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. Ref.9 Ref.11 Ref.12 Ref.13

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Ref.9 Ref.11.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

sdhBP070142EBI-371263,EBI-1035514

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Succinate dehydrogenase flavoprotein subunit
PRO_0000158652

Regions

Nucleotide binding14 – 196FAD
Nucleotide binding37 – 5216FAD
Nucleotide binding404 – 4052FAD

Sites

Active site2861Proton acceptor
Binding site2211FAD
Binding site2421Substrate
Binding site2541Substrate
Binding site3541Substrate
Binding site3881FAD
Binding site3991Substrate

Amino acid modifications

Modified residue451Tele-8alpha-FAD histidine
Modified residue2671N6-acetyllysine Ref.10

Experimental info

Sequence conflict20 – 223MRA → IAR in AAA23895. Ref.1
Sequence conflict20 – 223MRA → IAR in CAA25487. Ref.1

Secondary structure

............................................................................................................... 588
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AC41 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 837F9A63991B6CE8

FASTA58864,422
        10         20         30         40         50         60 
MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ GGITVALGNT 

        70         80         90        100        110        120 
HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE HMGLPFSRLD DGRIYQRPFG 

       130        140        150        160        170        180 
GQSKNFGGEQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAVVGC 

       190        200        210        220        230        240 
TALCIETGEV VYFKARATVL ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ 

       250        260        270        280        290        300 
FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG 

       310        320        330        340        350        360 
RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI PTCHYMMGGI 

       370        380        390        400        410        420 
PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL GGNSLLDLVV FGRAAGLHLQ 

       430        440        450        460        470        480 
ESIAEQGALR DASESDVEAS LDRLNRWNNN RNGEDPVAIR KALQECMQHN FSVFREGDAM 

       490        500        510        520        530        540 
AKGLEQLKVI RERLKNARLD DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH 

       550        560        570        580 
SRFDFPDRDD ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli."
Wood D., Darlison M.G., Wilde R.J., Guest J.R.
Biochem. J. 222:519-534(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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."
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. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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 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] OF 578-588.
Strain: K12.
[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 1-12.
Strain: K12 / EMG2.
[7]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-4.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[10]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[11]"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 FAD AND OXALOACETATE, ENZYME REGULATION, SUBCELLULAR LOCATION, SUBUNIT.
[12]"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 FAD AND OXALOACETATE, SUBUNIT.
[13]"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 FAD AND MALATE-LIKE INTERMEDIATE, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01619 Genomic DNA. Translation: AAA23895.1.
X00980 Genomic DNA. Translation: CAA25487.1.
U00096 Genomic DNA. Translation: AAC73817.1.
AP009048 Genomic DNA. Translation: BAA35390.1.
X01070 Genomic DNA. Translation: CAA25533.1.
PIRDEECSF. B64808.
RefSeqNP_415251.1. NC_000913.3.
YP_489003.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NEKX-ray2.60A1-588[»]
1NENX-ray2.90A1-588[»]
2ACZX-ray3.10A1-588[»]
2AD0model-A1-588[»]
2WDQX-ray2.40A/E/I1-588[»]
2WDRX-ray3.20A/E/I1-588[»]
2WDVX-ray3.20A/E/I1-588[»]
2WP9X-ray2.70A/E/I1-588[»]
2WS3X-ray3.20A/E/I1-588[»]
2WU2X-ray2.50A/E/I1-588[»]
2WU5X-ray2.80A/E/I1-588[»]
ProteinModelPortalP0AC41.
SMRP0AC41. Positions 1-588.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31877N.
IntActP0AC41. 91 interactions.
MINTMINT-6478272.
STRING511145.b0723.

2D gel databases

SWISS-2DPAGEP0AC41.

Proteomic databases

PaxDbP0AC41.
PRIDEP0AC41.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73817; AAC73817; b0723.
BAA35390; BAA35390; BAA35390.
GeneID12933913.
945402.
KEGGecj:Y75_p0703.
eco:b0723.
PATRIC32116641. VBIEscCol129921_0753.

Organism-specific databases

EchoBASEEB0924.
EcoGeneEG10931. sdhA.

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
KOK00239.
OMARTEQGRI.
OrthoDBEOG6M3PC4.
PhylomeDBP0AC41.

Enzyme and pathway databases

BioCycEcoCyc:SDH-FLAVO.
ECOL316407:JW0713-MONOMER.
MetaCyc:SDH-FLAVO.
UniPathwayUPA00223; UER01005.

Gene expression databases

GenevestigatorP0AC41.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AC41.
PROP0AC41.

Entry information

Entry nameSDHA_ECOLI
AccessionPrimary (citable) accession number: P0AC41
Secondary accession number(s): P10444, P78282
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: June 11, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene