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Protein

Sulfide-quinone reductase

Gene

AFE_1792

Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfur.2 Publications

Catalytic activityi

n sulfide + n quinone = polysulfide + n quinol.2 Publications

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Kineticsi

  1. KM=2.8 µM for sodium sulfide1 Publication
  2. KM=22 µM for decylubiquinone1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei160 – 1601Cysteine persulfide intermediate2 Publications
    Binding sitei302 – 3021FAD; via amide nitrogen2 Publications
    Binding sitei322 – 3221FAD; via amide nitrogen2 Publications
    Active sitei356 – 3561Cysteine persulfide intermediate2 Publications
    Binding sitei391 – 3911FAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi8 – 125FAD2 Publications
    Nucleotide bindingi34 – 352FAD2 Publications
    Nucleotide bindingi77 – 782FAD2 Publications

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciAFER243159:GH3S-1788-MONOMER.
    BRENDAi1.8.5.4. 91.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfide-quinone reductase (EC:1.8.5.42 Publications)
    Short name:
    SQR
    Alternative name(s):
    Sulfide:quinone oxidoreductase
    Gene namesi
    Ordered Locus Names:AFE_1792Imported
    OrganismiAcidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))Imported
    Taxonomic identifieri243159 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAcidithiobacilliaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus
    Proteomesi
    • UP000001362 Componenti: Chromosome

    Subcellular locationi

    • Membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi126 – 1261S → A: No effect on FAD reduction. Strongly reduced activity with decylubiquinone. 1 Publication
    Mutagenesisi128 – 1281C → A: No effect on FAD reduction. Strongly reduced activity with decylubiquinone. 2 Publications
    Mutagenesisi128 – 1281C → S: No effect on FAD reduction. Abolishes activity with decylubiquinone. 1 Publication
    Mutagenesisi132 – 1321H → A: No effect on FAD reduction. Reduced activity with decylubiquinone. 1 Publication
    Mutagenesisi160 – 1601C → A: Strongly reduces FAD reduction. Abolishes activity with decylubiquinone. 2 Publications
    Mutagenesisi198 – 1981H → A: No effect on FAD reduction. Reduced activity with decylubiquinone. 1 Publication
    Mutagenesisi356 – 3561C → A: Complete loss of enzyme activity. Abolishes enzyme FAD reduction. Abolishes activity with decylubiquinone. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Sulfide-quinone reductasePRO_0000430825Add
    BLAST

    Keywords - PTMi

    Quinone

    Proteomic databases

    PaxDbiB7JBP8.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi243159.AFE_1792.

    Structurei

    Secondary structure

    1
    434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75Combined sources
    Helixi13 – 2412Combined sources
    Helixi25 – 273Combined sources
    Beta strandi28 – 336Combined sources
    Beta strandi35 – 406Combined sources
    Helixi42 – 443Combined sources
    Helixi45 – 495Combined sources
    Helixi55 – 584Combined sources
    Beta strandi59 – 613Combined sources
    Helixi63 – 675Combined sources
    Turni68 – 703Combined sources
    Beta strandi72 – 743Combined sources
    Beta strandi78 – 825Combined sources
    Turni83 – 864Combined sources
    Beta strandi87 – 904Combined sources
    Beta strandi95 – 973Combined sources
    Beta strandi99 – 1035Combined sources
    Beta strandi107 – 1093Combined sources
    Helixi111 – 1133Combined sources
    Turni119 – 1213Combined sources
    Beta strandi122 – 1254Combined sources
    Helixi130 – 14516Combined sources
    Beta strandi150 – 1545Combined sources
    Helixi162 – 17716Combined sources
    Helixi181 – 1833Combined sources
    Beta strandi187 – 1959Combined sources
    Turni199 – 2024Combined sources
    Helixi207 – 21711Combined sources
    Beta strandi221 – 2233Combined sources
    Beta strandi225 – 2328Combined sources
    Beta strandi235 – 2417Combined sources
    Beta strandi247 – 2548Combined sources
    Beta strandi256 – 2616Combined sources
    Beta strandi264 – 2663Combined sources
    Helixi268 – 2714Combined sources
    Turni274 – 2763Combined sources
    Beta strandi289 – 2935Combined sources
    Beta strandi297 – 2993Combined sources
    Helixi301 – 3033Combined sources
    Helixi322 – 33918Combined sources
    Turni340 – 3423Combined sources
    Beta strandi354 – 3596Combined sources
    Beta strandi364 – 37512Combined sources
    Beta strandi377 – 3848Combined sources
    Helixi385 – 40420Combined sources
    Beta strandi408 – 4103Combined sources
    Helixi413 – 4164Combined sources
    Turni423 – 4264Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KPKX-ray2.05A1-434[»]
    3SX6X-ray1.80A2-434[»]
    3SXIX-ray2.18A2-434[»]
    3SY4X-ray1.91A2-434[»]
    3SYIX-ray2.20A2-434[»]
    3SZ0X-ray2.15A2-434[»]
    3SZCX-ray2.20A2-434[»]
    3SZFX-ray2.10A2-434[»]
    3SZWX-ray2.20A2-434[»]
    3T0KX-ray2.00A2-434[»]
    3T14X-ray2.21A2-434[»]
    3T2KX-ray2.35A2-434[»]
    3T2YX-ray2.50A1-434[»]
    3T2ZX-ray2.30A/B2-434[»]
    3T31X-ray2.30A2-434[»]
    ProteinModelPortaliB7JBP8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiB7JBP8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SQRD family.Curated

    Phylogenomic databases

    eggNOGiENOG4107SA8. Bacteria.
    COG0446. LUCA.
    HOGENOMiHOG000008171.
    KOiK17218.
    OMAiAYEFAFI.
    OrthoDBiEOG67T5FN.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    B7JBP8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAHVVILGAG TGGMPAAYEM KEALGSGHEV TLISANDYFQ FVPSNPWVGV
    60 70 80 90 100
    GWKERDDIAF PIRHYVERKG IHFIAQSAEQ IDAEAQNITL ADGNTVHYDY
    110 120 130 140 150
    LMIATGPKLA FENVPGSDPH EGPVQSICTV DHAERAFAEY QALLREPGPI
    160 170 180 190 200
    VIGAMAGASC FGPAYEYAMI VASDLKKRGM RDKIPSFTFI TSEPYIGHLG
    210 220 230 240 250
    IQGVGDSKGI LTKGLKEEGI EAYTNCKVTK VEDNKMYVTQ VDEKGETIKE
    260 270 280 290 300
    MVLPVKFGMM IPAFKGVPAV AGVEGLCNPG GFVLVDEHQR SKKYANIFAA
    310 320 330 340 350
    GIAIAIPPVE TTPVPTGAPK TGYMIESMVS AAVHNIKADL EGRKGEQTMG
    360 370 380 390 400
    TWNAVCFADM GDRGAAFIAL PQLKPRKVDV FAYGRWVHLA KVAFEKYFIR
    410 420 430
    KMKMGVSEPF YEKVLFKMMG ITRLKEEDTH RKAS
    Length:434
    Mass (Da):47,406
    Last modified:February 10, 2009 - v1
    Checksum:iFEADC108550141FB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP001219 Genomic DNA. Translation: ACK80359.1.
    RefSeqiWP_012536761.1. NC_011761.1.

    Genome annotation databases

    EnsemblBacteriaiACK80359; ACK80359; AFE_1792.
    KEGGiafr:AFE_1792.
    PATRICi20654729. VBIAciFer29821_1636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP001219 Genomic DNA. Translation: ACK80359.1.
    RefSeqiWP_012536761.1. NC_011761.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KPKX-ray2.05A1-434[»]
    3SX6X-ray1.80A2-434[»]
    3SXIX-ray2.18A2-434[»]
    3SY4X-ray1.91A2-434[»]
    3SYIX-ray2.20A2-434[»]
    3SZ0X-ray2.15A2-434[»]
    3SZCX-ray2.20A2-434[»]
    3SZFX-ray2.10A2-434[»]
    3SZWX-ray2.20A2-434[»]
    3T0KX-ray2.00A2-434[»]
    3T14X-ray2.21A2-434[»]
    3T2KX-ray2.35A2-434[»]
    3T2YX-ray2.50A1-434[»]
    3T2ZX-ray2.30A/B2-434[»]
    3T31X-ray2.30A2-434[»]
    ProteinModelPortaliB7JBP8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243159.AFE_1792.

    Proteomic databases

    PaxDbiB7JBP8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACK80359; ACK80359; AFE_1792.
    KEGGiafr:AFE_1792.
    PATRICi20654729. VBIAciFer29821_1636.

    Phylogenomic databases

    eggNOGiENOG4107SA8. Bacteria.
    COG0446. LUCA.
    HOGENOMiHOG000008171.
    KOiK17218.
    OMAiAYEFAFI.
    OrthoDBiEOG67T5FN.

    Enzyme and pathway databases

    BioCyciAFER243159:GH3S-1788-MONOMER.
    BRENDAi1.8.5.4. 91.

    Miscellaneous databases

    EvolutionaryTraceiB7JBP8.

    Family and domain databases

    Gene3Di3.50.50.60. 3 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications."
      Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S.
      BMC Genomics 9:597-597(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455Imported.
    2. "Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfidotrophic respiration and detoxification."
      Cherney M.M., Zhang Y., Solomonson M., Weiner J.H., James M.N.
      J. Mol. Biol. 398:292-305(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FAD; UBIQUINONE AND HYDROGEN SULFIDE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-128; CYS-160 AND CYS-356.
    3. "Structure-activity characterization of sulfide:quinone oxidoreductase variants."
      Cherney M.M., Zhang Y., James M.N., Weiner J.H.
      J. Struct. Biol. 178:319-328(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-434 IN COMPLEX WITH FAD; UBIQUINONE AND HYDROGEN SULFIDE, ACTIVE SITE, MUTAGENESIS OF SER-126; CYS-128; HIS-132; CYS-160; HIS-198 AND CYS-356.

    Entry informationi

    Entry nameiSQRD_ACIF2
    AccessioniPrimary (citable) accession number: B7JBP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: February 10, 2009
    Last modified: April 13, 2016
    This is version 52 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, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.