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UniProtKB/Swiss-Prot entry Q2S5G4


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

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Entry information
Entry name CYSH_SALRD
Primary accession number Q2S5G4
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on January 24, 2006 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 26)
Name and origin of the protein
Protein name Phosphoadenosine phosphosulfate reductase
Synonyms EC 1.8.4.8
PAPS reductase, thioredoxin dependent
PAdoPS reductase
3'-phosphoadenylylsulfate reductase
PAPS sulfotransferase
Gene name
Name: cysH
OrderedLocusNames: SRU_0422
From
Salinibacter ruber (strain DSM 13855) [TaxID: 309807] [HAMAP proteome]
Taxonomy Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales; Sphingobacteriales genera incertae sedis; Salinibacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0509073102; PubMed=16330755 [NCBI, ExPASy, EBI, Israel, Japan]
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.;
"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea.";
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
Comments
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
CP000159; ABC44343.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_444567.1; -.
3D structure databases
ModBase Q2S5G4.
Enzyme and pathway databases
BioCyc SRUB309807:SRU_0422-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004604; Molecular function: phosphoadenylyl-sulfate reductase (thioredoxin) activity (inferred from electronic annotation from HAMAP).
GO:0019379; Biological process: sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00063; -; 1.
PBIL [Tree]
InterPro IPR004511; CysH.
IPR002500; PAPS_reduct.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF01507; PAPS_reduct; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00434; cysH; 1.
BLOCKS Q2S5G4.
Genome annotation databases
GeneID 3852402; -.
GenomeReviews CP000159_GR; SRU_0422.
KEGG sru:SRU_0422; -.
NMPDR fig|309807.5.peg.387; -.
TIGR SRU_0422; -.
Phylogenomic databases
HOGENOM Q2S5G4; -.
Other
ProtoNet Q2S5G4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   252  252     Phosphoadenosine phosphosulfate reductase. PRO_1000075076
Sequence information
Length: 252 AA [This is the length of the unprocessed precursor] Molecular weight: 28593 Da [This is the MW of the unprocessed precursor] CRC64: 2007E8A7AB199D84 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAFASDESAS PWSSTRLAAL NAQFEPHGPK AILNWATHTF GDDLAQGTGF GPSGIVIMHM 

        70         80         90        100        110        120 
LADLRPGTTV FYLDTDLLFP ETYELCDDLD ERLDVDVTRV HGGLSLDEQA EQEGEELWNR 

       130        140        150        160        170        180 
NPNRCCFLRK VKPLRNFLDD RRAWITGVRR DQSERRADTD ILSWEGQYGV FKINPLANWT 

       190        200        210        220        230        240 
QKEVWKYLFE HDLPYNPKHD QGYPSLGCVP CTEPVDQADG YSREGRWSDR DKTECGLHTS 

       250 
PEDEDGAHAA ES 

Q2S5G4 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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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

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