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P0AC41

- SDHA_ECOLI

UniProt

P0AC41 - SDHA_ECOLI

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Protein

Succinate dehydrogenase flavoprotein subunit

Gene

sdhA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

FAD.1 Publication

Enzyme regulationi

Inhibited by oxaloacetate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei221 – 2211FAD3 Publications
Binding sitei242 – 2421Substrate
Binding sitei254 – 2541Substrate
Active sitei286 – 2861Proton acceptor
Binding sitei354 – 3541Substrate
Binding sitei388 – 3881FAD3 Publications
Binding sitei399 – 3991Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 196FAD3 Publications
Nucleotide bindingi37 – 5216FAD3 PublicationsAdd
BLAST
Nucleotide bindingi404 – 4052FAD3 Publications

GO - Molecular functioni

  1. electron carrier activity Source: EcoCyc
  2. flavin adenine dinucleotide binding Source: EcoliWiki
  3. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  4. succinate dehydrogenase activity Source: EcoliWiki

GO - Biological processi

  1. aerobic respiration Source: EcoliWiki
  2. electron transport chain Source: InterPro
  3. oxidation-reduction process Source: EcoliWiki
  4. tricarboxylic acid cycle Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:SDH-FLAVO.
ECOL316407:JW0713-MONOMER.
MetaCyc:SDH-FLAVO.
UniPathwayiUPA00223; UER01005.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase flavoprotein subunit (EC:1.3.5.1)
Gene namesi
Name:sdhA
Ordered Locus Names:b0723, JW0713
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10931. sdhA.

Subcellular locationi

Cell inner membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side 2 Publications

GO - Cellular componenti

  1. plasma membrane Source: EcoliWiki
  2. plasma membrane succinate dehydrogenase complex Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 588588Succinate dehydrogenase flavoprotein subunitPRO_0000158652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451Tele-8alpha-FAD histidine
Modified residuei267 – 2671N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AC41.
PRIDEiP0AC41.

2D gel databases

SWISS-2DPAGEP0AC41.

Expressioni

Gene expression databases

GenevestigatoriP0AC41.

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
sdhBP070142EBI-371263,EBI-1035514

Protein-protein interaction databases

DIPiDIP-31877N.
IntActiP0AC41. 91 interactions.
MINTiMINT-6478272.
STRINGi511145.b0723.

Structurei

Secondary structure

1
588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139
Helixi17 – 2812
Beta strandi33 – 397
Helixi41 – 433
Helixi45 – 484
Beta strandi59 – 613
Helixi65 – 7511
Turni76 – 783
Helixi82 – 10120
Beta strandi112 – 1143
Beta strandi119 – 1213
Turni125 – 1273
Beta strandi129 – 1357
Helixi141 – 15515
Beta strandi159 – 1624
Beta strandi164 – 1718
Beta strandi177 – 1848
Turni185 – 1873
Beta strandi190 – 20011
Helixi206 – 2083
Beta strandi209 – 2146
Helixi221 – 2288
Beta strandi233 – 2353
Beta strandi239 – 2468
Turni247 – 2493
Helixi256 – 2594
Beta strandi263 – 2653
Helixi273 – 2764
Turni278 – 2803
Helixi281 – 2833
Helixi286 – 29813
Beta strandi305 – 3073
Beta strandi309 – 3146
Helixi316 – 3183
Helixi319 – 3268
Helixi328 – 33710
Turni342 – 3443
Beta strandi347 – 35610
Beta strandi359 – 3624
Beta strandi367 – 3715
Beta strandi373 – 3753
Beta strandi377 – 3859
Helixi387 – 3893
Beta strandi393 – 3953
Helixi403 – 41715
Helixi419 – 4268
Helixi434 – 4396
Helixi442 – 4498
Beta strandi452 – 4543
Helixi456 – 47015
Beta strandi471 – 4755
Helixi477 – 49418
Beta strandi504 – 5063
Helixi508 – 53225
Beta strandi542 – 5454
Helixi550 – 5534
Beta strandi554 – 5607
Turni561 – 5644
Beta strandi565 – 5695
Beta strandi576 – 5783

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0AC41.
SMRiP0AC41. Positions 1-588.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC41.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1053.
HOGENOMiHOG000160475.
InParanoidiP0AC41.
KOiK00239.
OMAiRTEQGRI.
OrthoDBiEOG6M3PC4.
PhylomeDBiP0AC41.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. 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]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AC41-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ
60 70 80 90 100
GGITVALGNT HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE
110 120 130 140 150
HMGLPFSRLD DGRIYQRPFG GQSKNFGGEQ AARTAAAADR TGHALLHTLY
160 170 180 190 200
QQNLKNHTTI FSEWYALDLV KNQDGAVVGC TALCIETGEV VYFKARATVL
210 220 230 240 250
ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ FHPTGIAGAG
260 270 280 290 300
VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG
310 320 330 340 350
RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI
360 370 380 390 400
PTCHYMMGGI PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL
410 420 430 440 450
GGNSLLDLVV FGRAAGLHLQ ESIAEQGALR DASESDVEAS LDRLNRWNNN
460 470 480 490 500
RNGEDPVAIR KALQECMQHN FSVFREGDAM AKGLEQLKVI RERLKNARLD
510 520 530 540 550
DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH SRFDFPDRDD
560 570 580
ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY
Length:588
Mass (Da):64,422
Last modified:November 8, 2005 - v1
Checksum:i837F9A63991B6CE8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 223MRA → IAR in AAA23895. (PubMed:6383359)Curated
Sequence conflicti20 – 223MRA → IAR in CAA25487. (PubMed:6383359)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiB64808. DEECSF.
RefSeqiNP_415251.1. NC_000913.3.
YP_489003.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73817; AAC73817; b0723.
BAA35390; BAA35390; BAA35390.
GeneIDi12933913.
945402.
KEGGiecj:Y75_p0703.
eco:b0723.
PATRICi32116641. VBIEscCol129921_0753.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi B64808. DEECSF.
RefSeqi NP_415251.1. NC_000913.3.
YP_489003.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0AC41.
SMRi P0AC41. Positions 1-588.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31877N.
IntActi P0AC41. 91 interactions.
MINTi MINT-6478272.
STRINGi 511145.b0723.

2D gel databases

SWISS-2DPAGE P0AC41.

Proteomic databases

PaxDbi P0AC41.
PRIDEi P0AC41.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73817 ; AAC73817 ; b0723 .
BAA35390 ; BAA35390 ; BAA35390 .
GeneIDi 12933913.
945402.
KEGGi ecj:Y75_p0703.
eco:b0723.
PATRICi 32116641. VBIEscCol129921_0753.

Organism-specific databases

EchoBASEi EB0924.
EcoGenei EG10931. sdhA.

Phylogenomic databases

eggNOGi COG1053.
HOGENOMi HOG000160475.
InParanoidi P0AC41.
KOi K00239.
OMAi RTEQGRI.
OrthoDBi EOG6M3PC4.
PhylomeDBi P0AC41.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01005 .
BioCyci EcoCyc:SDH-FLAVO.
ECOL316407:JW0713-MONOMER.
MetaCyc:SDH-FLAVO.

Miscellaneous databases

EvolutionaryTracei P0AC41.
PROi P0AC41.

Gene expression databases

Genevestigatori P0AC41.

Family and domain databases

Gene3Di 1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProi IPR003953. 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 ]
Pfami PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsi TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEi PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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 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. 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. 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.

Entry informationi

Entry nameiSDHA_ECOLI
AccessioniPrimary (citable) accession number: P0AC41
Secondary accession number(s): P10444, P78282
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: October 29, 2014
This is version 88 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