Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot O33579 (CYSH_RHITR)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoadenosine phosphosulfate reductase
    EC=1.8.4.8
Alternative name(s):
    PAPS reductase, thioredoxin dependent
    PAdoPS reductase
    3'-phosphoadenylylsulfate reductase
    PAPS sulfotransferase
Gene names
Name: cysH
OrganismRhizobium tropici
Taxonomic identifier398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length180 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

Sequence similarities

Belongs to the PAPS reductase family. CysH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 180›180Phosphoadenosine phosphosulfate reductase HAMAP MF_00063
PRO_0000100641

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
O33579-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F948C70505E461F4

FASTA18020,395
        10         20         30         40         50         60 
LQTGRLFPET LKLIDETENQ YDIRISRYEP EQADIDAYAE KYGLNGFYES VEARHACCGV 

        70         80         90        100        110        120 
RKLKPLARAL SGATIWVTGL RRGQSANRAD TPFAEYDPER NLIKVNPLAD WDIDVIRAYV 

       130        140        150        160        170        180 
ADNGVPVNPL HQRGYPSIGC EPCTRAIKPG EPERAGRWWW ENDEKRECGL HVHEEAAAAQ 

« Hide

References

[1]"Isolation and sequencing of a second Rhizobium tropici CFN299 genetic locus that contains genes homologous to amino acid sulphate activation genes."
Laeremans T., Martinez-Romero E., Vanderleyden J.
DNA Seq. 9:65-70(1998) [PubMed: 9773278] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CFN 299.

Cross-references

Sequence databases

AJ001223 Genomic DNA. Translation: CAA04617.1.

3D structure databases

HSSPHSSP built from PDB template 1SUR based on UniProtKB P17854.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.4.8. 258207.

Family and domain databases

HAMAPMF_00063.
[Tree]
InterProIPR011798. APS_reductase.
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.
PfamPF01507. PAPS_reduct. 1 hit.
[Graphical view]
TIGRFAMsTIGR02055. APS_reductase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCYSH_RHITR
AccessionPrimary (citable) accession number: O33579
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents