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Q939U1

- SOXA_RHOSU

UniProt

Q939U1 - SOXA_RHOSU

Protein

SoxAX cytochrome complex subunit A

Gene

soxA

Organism
Rhodovulum sulfidophilum (Rhodobacter sulfidophilus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c and which then may be used for reductive CO2 fixation.4 Publications

    Cofactori

    Binds 2 heme groups per subunit.4 Publications

    Redox potential

    E0 is approximately -340 mV for His/Cys- ligated heme (heme 1) and -400 mV for His/CysS- ligated heme (heme 2) at pH 7.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei102 – 1021Heme 1 (covalent)2 PublicationsPROSITE-ProRule annotation
    Binding sitei105 – 1051Heme 1 (covalent)2 PublicationsPROSITE-ProRule annotation
    Metal bindingi106 – 1061Iron (heme 1 axial ligand); via tele nitrogen2 PublicationsPROSITE-ProRule annotation
    Metal bindingi140 – 1401Iron (heme 1 axial ligand)2 PublicationsPROSITE-ProRule annotation
    Binding sitei203 – 2031Heme 2 (covalent)2 PublicationsPROSITE-ProRule annotation
    Binding sitei206 – 2061Heme 2 (covalent)2 PublicationsPROSITE-ProRule annotation
    Metal bindingi207 – 2071Iron (heme 2 axial ligand); via tele nitrogen2 PublicationsPROSITE-ProRule annotation
    Binding sitei244 – 2441Substrate1 Publication
    Active sitei248 – 2481Cysteine persulfide intermediate2 Publications
    Metal bindingi248 – 2481Iron (heme 2 axial ligand)2 PublicationsPROSITE-ProRule annotation

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. heme binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. oxidoreductase activity Source: UniProtKB
    5. oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein heterodimerization activity Source: UniProtKB
    8. sulfurtransferase activity Source: UniProtKB

    GO - Biological processi

    1. enzyme active site formation via L-cysteine persulfide Source: UniProtKB
    2. oxidation-reduction process Source: UniProtKB
    3. sulfide oxidation Source: UniProtKB
    4. sulfur oxidation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SoxAX cytochrome complex subunit A2 Publications (EC:1.8.2.-1 Publication)
    Alternative name(s):
    Cytochrome c551 subunit dihemeImported1 Publication
    Protein SoxA1 Publication
    Sulfur oxidizing protein A1 Publication
    Thiosulfate-oxidizing multienzyme system protein SoxA2 Publications
    Short name:
    TOMES protein SoxA2 Publications
    Gene namesi
    Name:soxAImported
    OrganismiRhodovulum sulfidophilum (Rhodobacter sulfidophilus)
    Taxonomic identifieri35806 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodovulum

    Subcellular locationi

    Periplasm 1 Publication

    GO - Cellular componenti

    1. cytochrome complex Source: UniProtKB
    2. periplasmic space Source: UniProtKB

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Disruption phenotypei

    Unable to grow photoautotrophically on or oxidize either thiosulfate or sulfide. Thiosulfate:cytochrome c oxidoreductase activity is zero in periplasmic extracts prepared from cells grown on thiosulfate plus malate.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 287261SoxAX cytochrome complex subunit A1 PublicationPRO_0000423489Add
    BLAST

    Post-translational modificationi

    Cysteine persulfide at Cys-248.2 Publications

    Expressioni

    Inductioni

    By thiosulfate.1 Publication

    Interactioni

    Subunit structurei

    Heterodimer of SoxA and SoxX.3 Publications

    Structurei

    Secondary structure

    1
    287
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 343
    Turni35 – 373
    Beta strandi38 – 403
    Beta strandi43 – 453
    Helixi48 – 503
    Turni51 – 533
    Beta strandi55 – 584
    Helixi60 – 634
    Helixi66 – 716
    Helixi75 – 773
    Helixi80 – 9112
    Helixi102 – 1065
    Helixi109 – 1124
    Turni113 – 1153
    Helixi116 – 1194
    Beta strandi121 – 1233
    Turni125 – 1273
    Beta strandi128 – 1314
    Helixi133 – 14311
    Helixi155 – 16612
    Turni167 – 1704
    Helixi179 – 1813
    Helixi182 – 19211
    Turni197 – 2004
    Helixi203 – 2075
    Beta strandi213 – 2153
    Beta strandi229 – 2324
    Turni233 – 2364
    Beta strandi237 – 2393
    Helixi241 – 25010
    Turni251 – 2533
    Helixi262 – 27413
    Turni275 – 2773
    Beta strandi278 – 2803
    Beta strandi283 – 2864

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H31X-ray2.55A/C/E/G27-287[»]
    1H32X-ray1.50A27-287[»]
    1H33X-ray1.75A27-287[»]
    2OZ1X-ray2.35A/C/E/G27-287[»]
    ProteinModelPortaliQ939U1.
    SMRiQ939U1. Positions 27-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ939U1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini74 – 16895Cytochrome cPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SoxA family.CuratedSequence Analysis
    Contains 1 cytochrome c domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di1.10.760.10. 2 hits.
    InterProiIPR009056. Cyt_c-like_dom.
    IPR025710. SoxA.
    [Graphical view]
    PIRSFiPIRSF038455. SoxA. 1 hit.
    SUPFAMiSSF46626. SSF46626. 2 hits.
    PROSITEiPS51007. CYTC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q939U1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTMTGRLVA AALVCGGAFS GAAVSAGPDD PLVINGEIEI VTRAPTPAHL    50
    ADRFDEIRSG WTFRTDDTQA LEMDDFENSG MVFVEEARAV WDRPEGTEGK 100
    ACADCHGAVD DGMYGLRAVY PKYVESAGKV RTVEQMINAC RTSRMGAPEW 150
    DYIGPDMTAM VALIASVSRG MPVSVAIDGP AQSTWEKGRE IYYTRYGQLD 200
    LSCASCHEQY FDHYIRADHL SQGQINGFPS YRLKNARLNA VHDRFRGCIR 250
    DTRGVPFAVG SPEFVALELY VASRGNGLSV EGPSVRN 287
    Length:287
    Mass (Da):31,332
    Last modified:December 1, 2001 - v1
    Checksum:i95748C569D40853F
    GO

    Mass spectrometryi

    Molecular mass is 30177±4 Da from positions 27 - 287. Determined by ESI. The measured mass is that of mature SoxA with a diheme bound and with an undetermined modification.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY005800 Genomic DNA. Translation: AAF99434.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY005800 Genomic DNA. Translation: AAF99434.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H31 X-ray 2.55 A/C/E/G 27-287 [» ]
    1H32 X-ray 1.50 A 27-287 [» ]
    1H33 X-ray 1.75 A 27-287 [» ]
    2OZ1 X-ray 2.35 A/C/E/G 27-287 [» ]
    ProteinModelPortali Q939U1.
    SMRi Q939U1. Positions 27-287.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q939U1.

    Family and domain databases

    Gene3Di 1.10.760.10. 2 hits.
    InterProi IPR009056. Cyt_c-like_dom.
    IPR025710. SoxA.
    [Graphical view ]
    PIRSFi PIRSF038455. SoxA. 1 hit.
    SUPFAMi SSF46626. SSF46626. 2 hits.
    PROSITEi PS51007. CYTC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cytochrome complex essential for photosynthetic oxidation of both thiosulfate and sulfide in Rhodovulum sulfidophilum."
      Appia-Ayme C., Little P.J., Matsumoto Y., Leech A.P., Berks B.C.
      J. Bacteriol. 183:6107-6118(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-57; 66-73; 132-139; 255-266 AND 274-287, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION BY THIOSULFATE, MASS SPECTROMETRY, DISRUPTION PHENOTYPE, SIGNAL.
      Strain: W41 Publication.
    2. "Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum."
      Cheesman M.R., Little P.J., Berks B.C.
      Biochemistry 40:10562-10569(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, EPR SPECTROSCOPY OF THE HEMES, MAGNETIC CIRCULAR DICHROISM OF THE SOXAX COMPLEX.
      Strain: W41 Publication.
    3. "Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme."
      Bamford V.A., Bruno S., Rasmussen T., Appia-Ayme C., Cheesman M.R., Berks B.C., Hemmings A.M.
      EMBO J. 21:5599-5610(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-287 IN COMPLEXES WITH SOXX IN OXIDIZED AND REDUCED STATES AND HEMES, FUNCTION, COFACTOR, SUBUNIT, EPR SPECTROSCOPY OF THE HEMES, REACTION MECHANISM, ACTIVE SITE, CYSTEINE PERSULFIDE AT CYS-248.
      Strain: W41 Publication.
    4. "Redox and chemical activities of the hemes in the sulfur oxidation pathway enzyme SoxAX."
      Bradley J.M., Marritt S.J., Kihlken M.A., Haynes K., Hemmings A.M., Berks B.C., Cheesman M.R., Butt J.N.
      J. Biol. Chem. 287:40350-40359(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-287 IN COMPLEX WITH SOXX AND HEME, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, POTENTIOMETRIC TITRATION; EPR SPECTROSCOPY AND MAGNETIC CIRCULAR DICHROISM OF THE SOXAX COMPLEX, REACTION MECHANISM, ACTIVE SITE, CYSTEINE PERSULFIDE AT CYS-248.
      Strain: W41 Publication.

    Entry informationi

    Entry nameiSOXA_RHOSU
    AccessioniPrimary (citable) accession number: Q939U1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 18, 2013
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    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, Direct protein sequencing

    Documents

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

    External Data

    Dasty 3