Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Active sitei160Cysteine persulfide intermediate2 Publications1
    Binding sitei302FAD; via amide nitrogen2 Publications1
    Binding sitei322FAD; via amide nitrogen2 Publications1
    Active sitei356Cysteine persulfide intermediate2 Publications1
    Binding sitei391FAD2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi8 – 12FAD2 Publications5
    Nucleotide bindingi34 – 35FAD2 Publications2
    Nucleotide bindingi77 – 78FAD2 Publications2

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi126S → A: No effect on FAD reduction. Strongly reduced activity with decylubiquinone. 1 Publication1
    Mutagenesisi128C → A: No effect on FAD reduction. Strongly reduced activity with decylubiquinone. 2 Publications1
    Mutagenesisi128C → S: No effect on FAD reduction. Abolishes activity with decylubiquinone. 1 Publication1
    Mutagenesisi132H → A: No effect on FAD reduction. Reduced activity with decylubiquinone. 1 Publication1
    Mutagenesisi160C → A: Strongly reduces FAD reduction. Abolishes activity with decylubiquinone. 2 Publications1
    Mutagenesisi198H → A: No effect on FAD reduction. Reduced activity with decylubiquinone. 1 Publication1
    Mutagenesisi356C → A: Complete loss of enzyme activity. Abolishes enzyme FAD reduction. Abolishes activity with decylubiquinone. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004308251 – 434Sulfide-quinone reductaseAdd BLAST434

    Keywords - PTMi

    Quinone

    Proteomic databases

    PaxDbiB7JBP8.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi243159.AFE_1792.

    Structurei

    Secondary structure

    1434
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 7Combined sources5
    Helixi13 – 24Combined sources12
    Helixi25 – 27Combined sources3
    Beta strandi28 – 33Combined sources6
    Beta strandi35 – 40Combined sources6
    Helixi42 – 44Combined sources3
    Helixi45 – 49Combined sources5
    Helixi55 – 58Combined sources4
    Beta strandi59 – 61Combined sources3
    Helixi63 – 67Combined sources5
    Turni68 – 70Combined sources3
    Beta strandi72 – 74Combined sources3
    Beta strandi78 – 82Combined sources5
    Turni83 – 86Combined sources4
    Beta strandi87 – 90Combined sources4
    Beta strandi95 – 97Combined sources3
    Beta strandi99 – 103Combined sources5
    Beta strandi107 – 109Combined sources3
    Helixi111 – 113Combined sources3
    Turni119 – 121Combined sources3
    Beta strandi122 – 125Combined sources4
    Helixi130 – 145Combined sources16
    Beta strandi150 – 154Combined sources5
    Helixi162 – 177Combined sources16
    Helixi181 – 183Combined sources3
    Beta strandi187 – 195Combined sources9
    Turni199 – 202Combined sources4
    Helixi207 – 217Combined sources11
    Beta strandi221 – 223Combined sources3
    Beta strandi225 – 232Combined sources8
    Beta strandi235 – 241Combined sources7
    Beta strandi247 – 254Combined sources8
    Beta strandi256 – 261Combined sources6
    Beta strandi264 – 266Combined sources3
    Helixi268 – 271Combined sources4
    Turni274 – 276Combined sources3
    Beta strandi289 – 293Combined sources5
    Beta strandi297 – 299Combined sources3
    Helixi301 – 303Combined sources3
    Helixi322 – 339Combined sources18
    Turni340 – 342Combined sources3
    Beta strandi354 – 359Combined sources6
    Beta strandi364 – 375Combined sources12
    Beta strandi377 – 384Combined sources8
    Helixi385 – 404Combined sources20
    Beta strandi408 – 410Combined sources3
    Helixi413 – 416Combined sources4
    Turni423 – 426Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiB7JBP8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiB7JBP8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SQRD family.Curated

    Phylogenomic databases

    eggNOGiENOG4107SA8. Bacteria.
    COG0446. LUCA.
    HOGENOMiHOG000008171.
    KOiK17218.
    OMAiAYEFAFI.
    OrthoDBiPOG091H09D4.

    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
    PDB 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.
    SMRiB7JBP8.
    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.
    OrthoDBiPOG091H09D4.

    Enzyme and pathway databases

    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...

    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: November 2, 2016
    This is version 54 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.