Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0AC41

- SDHA_ECOLI

UniProt

P0AC41 - SDHA_ECOLI

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    4. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
    5. 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

    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

    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.
    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

    MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ    50
    GGITVALGNT HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE 100
    HMGLPFSRLD DGRIYQRPFG GQSKNFGGEQ AARTAAAADR TGHALLHTLY 150
    QQNLKNHTTI FSEWYALDLV KNQDGAVVGC TALCIETGEV VYFKARATVL 200
    ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ FHPTGIAGAG 250
    VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG 300
    RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI 350
    PTCHYMMGGI PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL 400
    GGNSLLDLVV FGRAAGLHLQ ESIAEQGALR DASESDVEAS LDRLNRWNNN 450
    RNGEDPVAIR KALQECMQHN FSVFREGDAM AKGLEQLKVI RERLKNARLD 500
    DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH SRFDFPDRDD 550
    ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY 588
    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.
    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

    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 1, 2014
    This is version 87 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