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UniProtKB/Swiss-Prot entry Q8FEI9

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

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Entry information
Entry name CYSH_ECOL6
Primary accession number Q8FEI9
Secondary accession numbers None
Integrated into Swiss-Prot on March 25, 2003
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 40)
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: c3321
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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
AE014075; AAN81770.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_755200.1; -.
3D structure databases
HSSP P17854; 1SUR. [HSSP ENTRY / PDB]
SMR Q8FEI9; 2-230.
ModBase Q8FEI9.
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.
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.
BLOCKS Q8FEI9.
Genome annotation databases
GeneID 1039150; -.
GenomeReviews AE014075_GR; c3321.
KEGG ecc:c3321; -.
Phylogenomic databases
HOGENOM Q8FEI9; -.
Genome annotation databases
CMR Q8FEI9; c3321.
Other
ProtoNet Q8FEI9.
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
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   244  243     Phosphoadenosine phosphosulfate reductase. PRO_0000100631
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 27975 Da [This is the MW of the unprocessed precursor] CRC64: A7101CF0F0B6AC7D [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 
SLHLVNQIRP 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 WEPGMAEEET RFFGLKRECG 


LHEG
Q8FEI9 in FASTA format

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