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UniProtKB/Swiss-Prot entry Q4L9F3


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

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Entry information
Entry name CYSH_STAHJ
Primary accession number Q4L9F3
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on August 2, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 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: SH0413
From
Staphylococcus haemolyticus (strain JCSC1435) [TaxID: 279808] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.21.7292-7308.2005; PubMed=16237012 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.;
"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species.";
J. Bacteriol. 187:7292-7308(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
AP006716; BAE03722.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_252328.1; -.
3D structure databases
ModBase Q4L9F3.
Enzyme and pathway databases
BioCyc SHAE279808:SH0413-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 IPR011798; APS_reductase.
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 TIGR02055; APS_reductase; 1.
TIGR00434; cysH; 1.
BLOCKS Q4L9F3.
Genome annotation databases
GeneID 3484069; -.
GenomeReviews AP006716_GR; SH0413.
KEGG sha:SH0413; -.
NMPDR fig|279808.3.peg.482; -.
Phylogenomic databases
HOGENOM Q4L9F3; -.
Genome annotation databases
CMR Q4L9F3; SH0413.
Other
ProtoNet Q4L9F3.
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   243  243     Phosphoadenosine phosphosulfate reductase. PRO_1000008941
Sequence information
Length: 243 AA [This is the length of the unprocessed precursor] Molecular weight: 28093 Da [This is the MW of the unprocessed precursor] CRC64: 27E3DAA32EE97BC4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVPTITYEN FEGDPFIDSI STDDATKGAY EILEWAYRTY GDSIVYSCSF GAESMVLIDL 

        70         80         90        100        110        120 
IYQIKPDAQI VFLDTDLHFQ ETYDLIDRVK EHFPKLRIEM KKPDLTLEEQ ADKYNPALWK 

       130        140        150        160        170        180 
NNPNQCCYIR KIKPLEEVLG GAVAWVSGLR RDQSPTRANT NFINKDERFK SVKVCPLIYW 

       190        200        210        220        230        240 
TEDEVWDYIK KHDLPYNALH DQHYPSIGCI PCTAPVFDSE DSRAGRWSNF DKTECGLHVA 


DKP 

Q4L9F3 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)
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