ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P29082

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SOR_ACIAM
Primary accession number P29082
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 50)
Name and origin of the protein
Protein name Sulfur oxygenase/reductase
Synonyms EC 1.13.11.55
Sulfur oxygenase reductase
SOR
Gene name
Name: sor
From
Acidianus ambivalens (Desulfurolobus ambivalens) [TaxID: 2283] 
Taxonomy Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Acidianus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29.
STRAIN=Lei 10 / DSM 3772 / JCM 9191;
PubMed=1522063 [NCBI, ExPASy, EBI, Israel, Japan]
Kletzin A.;
"Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens.";
J. Bacteriol. 174:5854-5859(1992).
[2]
 FUNCTION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, AND SUBUNIT.
DOI=10.1042/BJ20040003; PubMed=15030315 [NCBI, ExPASy, EBI, Israel, Japan]
Urich T., Bandeiras T.M., Leal S.S., Rachel R., Albrecht T., Zimmermann P., Scholz C., Teixeira M., Gomes C.M., Kletzin A.;
"The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre.";
Biochem. J. 381:137-146(2004).
[3]
 MUTAGENESIS OF CYS-31; HIS-86; HIS-90; CYS-101; CYS-104 AND GLU-114.
DOI=10.1016/j.femsle.2005.05.031; PubMed=15970399 [NCBI, ExPASy, EBI, Israel, Japan]
Urich T., Kroke A., Bauer C., Seyfarth K., Reuff M., Kletzin A.;
"Identification of core active site residues of the sulfur oxygenase reductase from Acidianus ambivalens by site-directed mutagenesis.";
FEMS Microbiol. Lett. 248:171-176(2005).
[4]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH IRON, SUBUNIT, PERSULFURATION AT CYS-31, AND REACTION MECHANISM.
DOI=10.1126/science.1120306; PubMed=16484493 [NCBI, ExPASy, EBI, Israel, Japan]
Urich T., Gomes C.M., Kletzin A., Frazao C.;
"X-ray structure of a self-compartmentalizing sulfur cycle metalloenzyme.";
Science 311:996-1000(2006).
Comments
  • FUNCTION: Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.
  • CATALYTIC ACTIVITY: 4 sulfur + 4 H2O + O2 = 2 H2S + 2 HSO3- + 2 H+.
  • COFACTOR: Binds 1 iron ion per subunit.
  • ENZYME REGULATION: Inhibited by zinc.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=23 mM for sulfur (at 65 degrees Celsius, with the oxygenase reaction);
    KM=13 mM for sulfur (at 65 degrees Celsius, with the reductase reaction);
  • SUBUNIT: Homoicosatetramer. The resulting structure is a hollow sphere where catalysis takes place in the inside cavity.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • INDUCTION: Aerobically induced.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X56616; CAA39952.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B43331; B43331.
3D structure databases
PDB
2CB2; X-ray; 1.70 A; A/B/C/D/E/F=1-309.[ExPASy / RCSB / EBI]
PDBsum 2CB2; -.
ModBase P29082.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12389; -.
Family and domain databases
InterPro IPR011661; S_Oase_red.
Graphical view of domain structure.
Pfam PF07682; SOR; 1.
Pfam graphical view of domain structure.
BLOCKS P29082.
Other
ProtoNet P29082.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   309  308     Sulfur oxygenase/reductase. PRO_0000072042
METAL   86    86        Iron; via tele nitrogen. 
METAL   90    90        Iron; via tele nitrogen. 
METAL   114   114        Iron. 
MOD_RES   31    31        Cysteine persulfide. 
MUTAGEN   31    31        C->A,S: No enzyme activity. Still binds iron. 
MUTAGEN   86    86        H->A: No enzyme activity and no iron bound. 
MUTAGEN   90    90        H->A: No enzyme activity and no iron bound. 
MUTAGEN   101   101        C->A: 10% residual activity. 
MUTAGEN   101   101        C->S: 1% residual enzyme activity, and no iron bound. 
MUTAGEN   104   104        C->A,S: 10% residual activity. 
MUTAGEN   114   114        E->A: No enzyme activity and no iron bound. 
MUTAGEN   114   114        E->D: 1% residual enzyme activity and 4% of wild-type levels of iron bound. 
STRAND   5    14  10      
HELIX   17    34  18      
STRAND   40    51  12      
TURN   54    60  7      
TURN   66    68  3      
STRAND   70    82  13      
HELIX   83    92  10      
HELIX   94   102  9      
HELIX   103   107  5      
STRAND   108   113  6      
STRAND   115   123  9      
TURN   130   132  3      
HELIX   133   142  10      
HELIX   146   148  3      
STRAND   156   168  13      
HELIX   173   187  15      
STRAND   193   204  12      
TURN   206   210  5      
HELIX   214   221  8      
STRAND   225   227  3      
HELIX   231   233  3      
HELIX   239   241  3      
STRAND   244   256  13      
HELIX   257   269  13      
HELIX   271   281  11      
STRAND   284   299  16      
HELIX   302   307  6      
Sequence information
Length: 309 AA [This is the length of the unprocessed precursor] Molecular weight: 35318 Da [This is the MW of the unprocessed precursor] CRC64: 95C0EEBF0AD079A6 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPKPYVAINM AELKNEPKTF EMFASVGPKV CMVTARHPGF VGFQNHIQIG ILPFGNRYGG 

        70         80         90        100        110        120 
AKMDMTKESS TVRVLQYTFW KDWKDHEEMH RQNWSYLFRL CYSCASQMIW GPWEPIYEII 

       130        140        150        160        170        180 
YANMPINTEM TDFTAVVGKK FAEGKPLDIP VISQPYGKRV VAFAEHSVIP GKEKQFEDAI 

       190        200        210        220        230        240 
VRTLEMLKKA PGFLGAMVLK EIGVSGIGSM QFGAKGFHQV LENPGSLEPD PNNVMYSVPE 

       250        260        270        280        290        300 
AKNTPQQYIV HVEWANTDAL MFGMGRVLLY PELRQVHDEV LDTLVYGPYI RILNPMMEGT 


FWREYLNEQ
P29082 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!