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UniProtKB/Swiss-Prot entry O05927

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

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Entry information
Entry name CYSH_PSEAE
Primary accession number O05927
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on December 8, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 65)
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: PA1756
From
Pseudomonas aeruginosa [TaxID: 287] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CHA;
PubMed=9218775 [NCBI, ExPASy, EBI, Israel, Japan]
Delic-Attree I., Toussaint B., Garin J., Vignais P.M.;
"Cloning, sequence and mutagenesis of the structural gene of Pseudomonas aeruginosa CysB, which can activate algD transcription.";
Mol. Microbiol. 24:1275-1284(1997).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).
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
U95379; AAB53743.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG05145.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H83426; H83426.
RefSeq NP_250447.1; -.
3D structure databases
PDB
2GOY; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-267.[ExPASy / RCSB / EBI]
PDBsum 2GOY; -.
ModBase O05927.
Enzyme and pathway databases
BioCyc PAER208964:PA1756-MON; -.
Organism-specific databases
PseudoCAP PA1756; -.
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 O05927.
Genome annotation databases
GeneID 878560; -.
GenomeReviews AE004091_GR; PA1756.
KEGG pae:PA1756; -.
NMPDR fig|208964.1.peg.1757; -.
Phylogenomic databases
HOGENOM O05927; -.
Genome annotation databases
CMR O05927; PA1756.
Other
ProtoNet O05927.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   267  267     Phosphoadenosine phosphosulfate reductase. PRO_0000100638
CONFLICT   2     2        L -> P (in Ref. 1; AAB53743). 
HELIX   33    36  4      
HELIX   42    53  12      
HELIX   54    56  3      
STRAND   58    60  3      
HELIX   67    76  10      
STRAND   81    85  5      
HELIX   92   105  14      
STRAND   110   112  3      
HELIX   116   126  11      
HELIX   131   134  4      
HELIX   137   143  7      
HELIX   145   151  7      
STRAND   156   159  4      
HELIX   164   166  3      
STRAND   176   179  4      
TURN   181   183  3      
STRAND   186   188  3      
STRAND   191   193  3      
TURN   195   198  4      
HELIX   201   210  10      
HELIX   217   220  4      
TURN   229   231  3      
HELIX   241   244  4      
Sequence information
Length: 267 AA [This is the length of the unprocessed precursor] Molecular weight: 30215 Da [This is the MW of the unprocessed precursor] CRC64: E9557E1970F21049 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLPFATIPAT ERNSAAQHQD PSPMSQPFDL PALASSLADK SPQDILKAAF EHFGDELWIS 

        70         80         90        100        110        120 
FSGAEDVVLV DMAWKLNRNV KVFSLDTGRL HPETYRFIDQ VREHYGIAID VLSPDPRLLE 

       130        140        150        160        170        180 
PLVKEKGLFS FYRDGHGECC GIRKIEPLKR KLAGVRAWAT GQRRDQSPGT RSQVAVLEID 

       190        200        210        220        230        240 
GAFSTPEKPL YKFNPLSSMT SEEVWGYIRM LELPYNSLHE RGYISIGCEP CTRPVLPNQH 

       250        260 
EREGRWWWEE ATHKECGLHA GNLISKA
O05927 in FASTA format

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