P0AC41 (DHSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
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.
Cofactor	FAD. Ref.12
Enzyme regulation	Inhibited by oxaloacetate. Ref.10
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 an hydrophobic anchor protein. The complex forms trimers. Ref.8 Ref.10 Ref.11 Ref.12
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Ref.8 Ref.10.
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	Cell inner membrane Cell membrane Membrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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 direct assay. Source: EcoliWiki
Cellular component	plasma membrane succinate dehydrogenase complex Inferred from direct assay Ref.8. Source: EcoliWiki
Molecular function	electron carrier activity Inferred from direct assay. Source: EcoCyc flavin adenine dinucleotide binding Inferred from direct assay Ref.10. Source: EcoliWiki protein binding Inferred from physical interaction Ref.10. Source: IntAct succinate dehydrogenase activity Inferred from mutant phenotype Ref.1. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
sdhB	P07014	3	EBI-371263,EBI-1035514

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

14 – 19

6

FAD

Nucleotide binding

37 – 52

16

FAD

Nucleotide binding

404 – 405

2

FAD

Sites

Active site

286

1

Proton acceptor

Binding site

221

1

FAD

Binding site

242

1

Substrate

Binding site

254

1

Substrate

Binding site

354

1

Substrate

Binding site

388

1

FAD

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

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588

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Beta strand

11 – 13

3

Helix

17 – 28

12

Beta strand

34 – 36

3

Helix

41 – 43

3

Helix

45 – 48

4

Beta strand

59 – 61

3

Helix

65 – 76

12

Helix

82 – 101

20

Beta strand

119 – 121

3

Beta strand

123 – 125

3

Beta strand

129 – 135

7

Helix

141 – 155

15

Beta strand

159 – 161

3

Beta strand

163 – 171

9

Beta strand

177 – 184

8

Turn

185 – 187

3

Beta strand

190 – 196

7

Beta strand

198 – 200

3

Helix

206 – 208

3

Beta strand

209 – 214

6

Helix

221 – 227

7

Turn

228 – 230

3

Beta strand

233 – 235

3

Beta strand

239 – 246

8

Turn

247 – 249

3

Helix

256 – 260

5

Beta strand

263 – 265

3

Helix

272 – 276

5

Turn

278 – 280

3

Helix

281 – 283

3

Helix

286 – 298

13

Beta strand

305 – 307

3

Beta strand

309 – 314

6

Helix

320 – 326

7

Helix

328 – 338

11

Turn

342 – 344

3

Beta strand

347 – 356

10

Beta strand

359 – 362

4

Beta strand

367 – 371

5

Beta strand

373 – 375

3

Beta strand

377 – 385

9

Beta strand

387 – 391

5

Beta strand

393 – 395

3

Helix

403 – 426

24

Helix

434 – 440

7

Helix

442 – 449

8

Beta strand

452 – 454

3

Helix

456 – 470

15

Beta strand

472 – 475

4

Helix

477 – 493

17

Helix

494 – 496

3

Helix

508 – 532

25

Beta strand

541 – 545

5

Turn

550 – 552

3

Beta strand

558 – 560

3

Beta strand

568 – 570

3

Sequences

	Sequence		Length	Mass (Da)
	P0AC41 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 837F9A63991B6CE8	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

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. , 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: 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. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[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.
[12]	"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: 19710024] [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.

PIR

DEECSF. B64808.

RefSeq

NP_415251.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
2WDQ	X-ray	2.40	A/E/I	1-588	[»]
2WDR	X-ray	3.20	A/E/I	1-588	[»]
2WDV	X-ray	3.20	A/E/I	1-588	[»]
2WP9	X-ray	2.70	A/E/I	1-588	[»]
2WS3	X-ray	3.20	A/E/I	1-588	[»]
2WU2	X-ray	2.50	A/E/I	1-588	[»]
2WU5	X-ray	2.80	A/E/I	1-588	[»]

ProteinModelPortal

P0AC41.

SMR

P0AC41. Positions 1-588.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AC41. 90 interactions.

2D gel databases

SWISS-2DPAGE

P0AC41.

ECO2DBASE

F060.3. 6TH EDITION.

Proteomic databases

PRIDE

P0AC41.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001155; EBESCP00000001155; EBESCG00000000952.
EBESCT00000001156; EBESCP00000001156; EBESCG00000000952.
EBESCT00000018021; EBESCP00000017312; EBESCG00000017077.

GeneID

945402.

GenomeReviews

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

KEGG

ecj:JW0713.
eco:b0723.

PATRIC

32116641. VBIEscCol129921_0753.

Organism-specific databases

EchoBASE

EB0924.

EcoGene

EG10931. sdhA.

Phylogenomic databases

eggNOG

COG1053.

GeneTree

EBGT00050000009824.

HOGENOM

HBG293998.

OMA

AHSRFDY.

PhylomeDB

P0AC41.

ProtClustDB

PRK08958.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0AC41.

Family and domain databases

InterPro

IPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]

Gene3D

G3DSA:1.20.58.100. Fum_Rdtase/Succ_DH_flav-like_C. 1 hit.

KO

K00239.

PANTHER

PTHR11632:SF5. PTHR11632:SF5. 1 hit.

Pfam

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

PRINTS

PR00368. FADPNR.

SUPFAM

SSF46977. Succ_DH_flav_C. 1 hit.

TIGRFAMs

TIGR01816. SdhA_forward. 1 hit.
TIGR01812. SdhA_frdA_Gneg. 1 hit.

PROSITE

PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program