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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

heme4 PublicationsNote: 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 heterodimerization activity Source: UniProtKB
  7. 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 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
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 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 – 343Combined sources
Turni35 – 373Combined sources
Beta strandi38 – 403Combined sources
Beta strandi43 – 453Combined sources
Helixi48 – 503Combined sources
Turni51 – 533Combined sources
Beta strandi55 – 584Combined sources
Helixi60 – 634Combined sources
Helixi66 – 716Combined sources
Helixi75 – 773Combined sources
Helixi80 – 9112Combined sources
Helixi102 – 1065Combined sources
Helixi109 – 1124Combined sources
Turni113 – 1153Combined sources
Helixi116 – 1194Combined sources
Beta strandi121 – 1233Combined sources
Turni125 – 1273Combined sources
Beta strandi128 – 1314Combined sources
Helixi133 – 14311Combined sources
Helixi155 – 16612Combined sources
Turni167 – 1704Combined sources
Helixi179 – 1813Combined sources
Helixi182 – 19211Combined sources
Turni197 – 2004Combined sources
Helixi203 – 2075Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi229 – 2324Combined sources
Turni233 – 2364Combined sources
Beta strandi237 – 2393Combined sources
Helixi241 – 25010Combined sources
Turni251 – 2533Combined sources
Helixi262 – 27413Combined sources
Turni275 – 2773Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi283 – 2864Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MKTMTGRLVA AALVCGGAFS GAAVSAGPDD PLVINGEIEI VTRAPTPAHL
60 70 80 90 100
ADRFDEIRSG WTFRTDDTQA LEMDDFENSG MVFVEEARAV WDRPEGTEGK
110 120 130 140 150
ACADCHGAVD DGMYGLRAVY PKYVESAGKV RTVEQMINAC RTSRMGAPEW
160 170 180 190 200
DYIGPDMTAM VALIASVSRG MPVSVAIDGP AQSTWEKGRE IYYTRYGQLD
210 220 230 240 250
LSCASCHEQY FDHYIRADHL SQGQINGFPS YRLKNARLNA VHDRFRGCIR
260 270 280
DTRGVPFAVG SPEFVALELY VASRGNGLSV EGPSVRN
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:
EMBLi
GenBanki
DDBJi
Links Updated
AY005800 Genomic DNA. Translation: AAF99434.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY005800 Genomic DNA. Translation: AAF99434.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 56 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