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O05927 (CYSH_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoadenosine phosphosulfate reductase
EC=1.8.4.8
Alternative name(s):
3'-phosphoadenylylsulfate reductase
PAPS reductase, thioredoxin dependent
PAPS sulfotransferase
PAdoPS reductase
Gene names
Name:cysH
Ordered Locus Names:PA1756
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduction of activated sulfate into sulfite. HAMAP MF_00063

Catalytic activity

Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. HAMAP MF_00063

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3. HAMAP MF_00063

Subcellular location

Cytoplasm By similarity HAMAP MF_00063.

Sequence similarities

Belongs to the PAPS reductase family. CysH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 267267Phosphoadenosine phosphosulfate reductase HAMAP MF_00063
PRO_0000100638

Experimental info

Sequence conflict21L → P in AAB53743. Ref.1

Secondary structure

1 ............................................. 267
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O05927 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: E9557E1970F21049

FASTA26730,215
        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

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence and mutagenesis of the structural gene of Pseudomonas aeruginosa CysB, which can activate algD transcription."
Delic-Attree I., Toussaint B., Garin J., Vignais P.M.
Mol. Microbiol. 24:1275-1284(1997) [PubMed: 9218775] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CHA.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
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. expand/collapse author list , 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.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U95379 Genomic DNA. Translation: AAB53743.1.
AE004091 Genomic DNA. Translation: AAG05145.1.
PIRH83426.
RefSeqNP_250447.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GOYX-ray2.70A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortalO05927.
SMRO05927. Positions 27-249.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID878560.
GenomeReviewsGene locus PA1756 in contig AE004091_GR.
KEGGpae:PA1756.
NMPDRfig|208964.1.peg.1757.
PATRIC19837867. VBIPseAer58763_1819.

Organism-specific databases

PseudoCAPPA1756.

Phylogenomic databases

HOGENOMHBG758022.
OMAAIHGTRF.
ProtClustDBPRK02090.

Enzyme and pathway databases

BioCycPAER208964:PA1756-MONOMER.
BRENDA1.8.4.10. 5087.

Family and domain databases

HAMAPMF_00063. CysH.
[Tree]
InterProIPR011798. APS_reductase.
IPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK00390.
PfamPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFPIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMsTIGR02055. APS_reductase. 1 hit.
TIGR00434. CysH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCYSH_PSEAE
AccessionPrimary (citable) accession number: O05927
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: January 25, 2012
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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