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Protein

SoxAX cytochrome complex subunit A

Gene

soxA

Organism
Rhodovulum sulfidophilum (Rhodobacter sulfidophilus)
Status
Reviewed-Annotation score: 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

Manual assertion based on experiment ini

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei102Heme 1 (covalent)PROSITE-ProRule annotation2 Publications1
Binding sitei105Heme 1 (covalent)PROSITE-ProRule annotation2 Publications1
Metal bindingi106Iron (heme 1 axial ligand); via tele nitrogenPROSITE-ProRule annotation2 Publications1
Metal bindingi140Iron (heme 1 axial ligand)PROSITE-ProRule annotation2 Publications1
Binding sitei203Heme 2 (covalent)PROSITE-ProRule annotation2 Publications1
Binding sitei206Heme 2 (covalent)PROSITE-ProRule annotation2 Publications1
Metal bindingi207Iron (heme 2 axial ligand); via tele nitrogenPROSITE-ProRule annotation2 Publications1
Binding sitei244Substrate1 Publication1
Active sitei248Cysteine persulfide intermediate2 Publications1
Metal bindingi248Iron (heme 2 axial ligand)PROSITE-ProRule annotation2 Publications1

GO - Molecular functioni

  • electron carrier activity Source: UniProtKB
  • heme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: UniProtKB
  • oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • sulfurtransferase activity Source: UniProtKB

GO - Biological processi

  • enzyme active site formation via cysteine modification to L-cysteine persulfide Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • sulfide oxidation Source: UniProtKB
  • 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 diheme1 PublicationImported
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

GO - Cellular componenti

  • cytochrome complex Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000042348927 – 287SoxAX cytochrome complex subunit A1 PublicationAdd BLAST261

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

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Structurei

Secondary structure

1287
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 34Combined sources3
Turni35 – 37Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi43 – 45Combined sources3
Helixi48 – 50Combined sources3
Turni51 – 53Combined sources3
Beta strandi55 – 58Combined sources4
Helixi60 – 63Combined sources4
Helixi66 – 71Combined sources6
Helixi75 – 77Combined sources3
Helixi80 – 91Combined sources12
Helixi102 – 106Combined sources5
Helixi109 – 112Combined sources4
Turni113 – 115Combined sources3
Helixi116 – 119Combined sources4
Beta strandi121 – 123Combined sources3
Turni125 – 127Combined sources3
Beta strandi128 – 131Combined sources4
Helixi133 – 143Combined sources11
Helixi155 – 166Combined sources12
Turni167 – 170Combined sources4
Helixi179 – 181Combined sources3
Helixi182 – 192Combined sources11
Turni197 – 200Combined sources4
Helixi203 – 207Combined sources5
Beta strandi213 – 215Combined sources3
Beta strandi229 – 232Combined sources4
Turni233 – 236Combined sources4
Beta strandi237 – 239Combined sources3
Helixi241 – 250Combined sources10
Turni251 – 253Combined sources3
Helixi262 – 274Combined sources13
Turni275 – 277Combined sources3
Beta strandi278 – 280Combined sources3
Beta strandi283 – 286Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ939U1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini74 – 168Cytochrome cPROSITE-ProRule annotationAdd BLAST95

Sequence similaritiesi

Belongs to the SoxA family.Sequence analysisCurated
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.
TIGRFAMsiTIGR04484. thiosulf_SoxA. 1 hit.
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.
RefSeqiWP_042460802.1. NZ_CP015421.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY005800 Genomic DNA. Translation: AAF99434.1.
RefSeqiWP_042460802.1. NZ_CP015421.1.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ939U1.

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.
TIGRFAMsiTIGR04484. thiosulf_SoxA. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 63 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

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.