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 Q32CG5


[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 CYSH_SHIDS
Primary accession number Q32CG5
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on December 6, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 22)
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: SDY_2964
From
Shigella dysenteriae serotype 1 (strain Sd197) [TaxID: 300267] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Shigella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gki954; PubMed=16275786 [NCBI, ExPASy, EBI, Israel, Japan]
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.;
"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery.";
Nucleic Acids Res. 33:6445-6458(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
CP000034; ABB62990.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_404481.1; -.
3D structure databases
SMR Q32CG5; 2-230.
ModBase Q32CG5.
Enzyme and pathway databases
BioCyc SDYS300267:SDY_2964-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:0016740; Molecular function: transferase activity (inferred from electronic annotation from InterPro).
GO:0019344; Biological process: cysteine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
IPR011800; PAPS_reductase.
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.
TIGR02057; PAPS_reductase; 1.
ProtoNet Q32CG5.
Genome annotation databases
GeneID 3796421; -.
GenomeReviews CP000034_GR; SDY_2964.
KEGG sdy:SDY_2964; -.
NMPDR fig|216598.1.peg.3739; -.
Phylogenomic databases
HOGENOM Q32CG5; -.
Genome annotation databases
CMR Q32CG5; SDY_2964.
Other
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   244  244     Phosphoadenosine phosphosulfate reductase. PRO_1000008937
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 27952 Da [This is the MW of the unprocessed precursor] CRC64: CC710DFC4101C719 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKLDLNALN ELPKVDRILA LAETNAQLEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV 

        70         80         90        100        110        120 
SLHLVNQICP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL 

       130        140        150        160        170        180 
WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL 

       190        200        210        220        230        240 
PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPSMAEEET RFFGLKRECG 


LHEG 

Q32CG5 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!