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Q939U1

- SOXA_RHOSU

UniProt

Q939U1 - SOXA_RHOSU

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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

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)
Binding sitei105 – 1051Heme 1 (covalent)
Metal bindingi106 – 1061Iron (heme 1 axial ligand); via tele nitrogen
Metal bindingi140 – 1401Iron (heme 1 axial ligand)
Binding sitei203 – 2031Heme 2 (covalent)
Binding sitei206 – 2061Heme 2 (covalent)
Metal bindingi207 – 2071Iron (heme 2 axial ligand); via tele nitrogen
Binding sitei244 – 2441Substrate
Active sitei248 – 2481Cysteine persulfide intermediate2 Publications
Metal bindingi248 – 2481Iron (heme 2 axial ligand)

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
Complete GO annotation...

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 A (EC:1.8.2.-)
Alternative name(s):
Cytochrome c551 subunit diheme
Protein SoxA
Sulfur oxidizing protein A
Thiosulfate-oxidizing multienzyme system protein SoxA
Short name:
TOMES protein SoxA
Gene namesi
Name:soxA
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
Complete GO annotation...

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 Publication
Add
BLAST
Chaini27 – 287261SoxAX cytochrome complex subunit A
PRO_0000423489Add
BLAST

Post-translational modificationi

Cysteine persulfide at Cys-248.

Expressioni

Inductioni

By thiosulfate.1 Publication

Interactioni

Subunit structurei

Heterodimer of SoxA and SoxX.3 Publications

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ939U1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 16895Cytochrome c
Add
BLAST

Sequence similaritiesi

Belongs to the SoxA family.

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

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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: W4.
  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: W4.
  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: W4.
  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: W4.

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: June 11, 2014
This is version 53 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

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