Succinate dehydrogenase flavoprotein subunit - Escherichia coli (strain K12)

Names and origin

Protein names

Recommended name:
Succinate dehydrogenase flavoprotein subunit
EC=1.3.99.1

Gene names

Name:	sdhA
Ordered Locus Names:	b0723, JW0713

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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 + acceptor = fumarate + reduced acceptor.
Enzyme regulation	Inhibited by oxaloacetate. Ref.10
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and an hydrophobic anchor protein. The complex forms trimers. Ref.10 Ref.8 Ref.11
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Ref.10 Ref.8
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct succinate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
dcuS	P0AEC8	1	EBI-371263,EBI-1134683
fliF	P25798	1	EBI-371263,EBI-1126492
nadE	P18843	1	EBI-371263,EBI-548960
narJ	P0AF26	1	EBI-371263,EBI-555043
paaG	P77467	1	EBI-371263,EBI-1118484
polB	P21189	1	EBI-371263,EBI-1113379

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 588

588

Succinate dehydrogenase flavoprotein subunit

PRO_0000158652

Regions

Nucleotide binding

37 – 52

16

FAD

Sites

Active site

286

1

Proton acceptor

Binding site

242

1

Substrate

Binding site

254

1

Substrate

Binding site

354

1

Substrate

Binding site

399

1

Substrate

Amino acid modifications

Modified residue

45

1

Tele-8alpha-FAD histidine

Modified residue

267

1

N6-acetyllysine Ref.9

Experimental info

Sequence conflict

20 – 22

3

MRA → IAR in AAA23895. Ref.1

Sequence conflict

20 – 22

3

MRA → IAR in CAA25487. Ref.1

Secondary structure

1

.

588

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P0AC41-1 [UniParc].

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

FASTA

588

64,422

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 6383359] [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. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 6388571] [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: 9298646] [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: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-4. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"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: 16079137] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION. Strain: BL21-DE3.
[9]	"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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, MASS SPECTROMETRY.
[10]	"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: 12560550] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, ENZYME REGULATION, SUBCELLULAR LOCATION, SUBUNIT.
[11]	"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: 16407191] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, SUBUNIT.

Hide | Top

Cross-references

Sequence databases

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.

PIR

DEECSF. B64808.

RefSeq

AP_001361.1.
NP_415251.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NEK	X-ray	2.60	A	1-588	[»]
1NEN	X-ray	2.90	A	1-588	[»]
2ACZ	X-ray	3.10	A	1-588	[»]
2AD0	model	-	A	1-588	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AC41. 90 interactions.

2-D gel databases

SWISS-2DPAGE

P0AC41.

ECO2DBASE

F060.3. 6TH EDITION.

Genome annotation databases

GeneID

945402.

GenomeReviews

Gene locus JW0713 in contig AP009048_GR.
Gene locus b0723 in contig U00096_GR.

KEGG

ecj:JW0713.
eco:b0723.

Organism-specific databases

EchoBASE

EB0924.

EcoGene

EG10931. sdhA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AC41.

OMA

P0AC41. TLEFDNL.

Enzyme and pathway databases

BioCyc

EcoCyc:SDH-FLAVO.
MetaCyc:SDH-FLAVO.

Family and domain databases

InterPro

IPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR003952. FRD_SDH_FAD_BS.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_frdA_Gneg.
[Graphical view]

Pfam

PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

TIGRFAMs

TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.

PROSITE

PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

Entry information

Entry name

DHSA_ECOLI

Accession

Primary (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 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents