Succinate dehydrogenase flavoprotein subunit - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0AC41 (DHSA_ECOLI)

Last modified June 10, 2008. Version 32. History...

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Names and origin · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Succinate dehydrogenase flavoprotein subunit
Also known as:
EC 1.3.99.1

Gene names

Name:	sdhA
Ordered Locus Names:	b0723, JW0713

Organism

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

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein existence

Evidence 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 + acceptor = fumarate + reduced acceptor.
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.
Subcellular location	Cell inner membrane; Peripheral membrane protein.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

588

Succinate dehydrogenase flavoprotein subunit

Regions

Nucleotide binding

15

FAD Potential

Sites

Active site

1

By similarity

Active site

1

By similarity

Amino acid modifications

Modified residue

1

Tele-8alpha-FAD histidine

Experimental info

Sequence conflict

3

MRA → IAR in AAA23895 and CAA25487. Ref.1

Secondary structure

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588

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P0AC41-1 [UniParc].

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

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

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.

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

Protein-protein interaction databases

IntAct

2-D gel databases

SWISS-2DPAGE

ECO2DBASE

F060.3. 6TH EDITION.

Genome annotation databases