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Q1R7T6 (CYSH_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:UTI89_C3126
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
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 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 – 244244Phosphoadenosine phosphosulfate reductase HAMAP MF_00063
PRO_1000008923

Sequences

Sequence LengthMass (Da)Tools
Q1R7T6 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: F91EFC1EFE48BC6B

FASTA24428,003
        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 NRALKELNVQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL 

       190        200        210        220        230        240 
PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG 


LHEG 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000243 Genomic DNA. Translation: ABE08578.1.
RefSeqYP_542109.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1R7T6.
SMRQ1R7T6. Positions 2-244.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1R7T6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000069240; EBESCP00000066718; EBESCG00000068287.
GeneID3990451.
GenomeReviewsGene locus UTI89_C3126 in contig CP000243_GR.
KEGGeci:UTI89_C3126.
PATRIC18455772. VBIEscCol42261_3108.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0175.
GeneTreeEBGT00050000009832.
HOGENOMHBG758022.
OMAAIHGTRF.
ProtClustDBPRK02090.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C3126-MONOMER.

Family and domain databases

HAMAPMF_00063. CysH.
[Tree]
InterProIPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
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]
TIGRFAMsTIGR00434. CysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCYSH_ECOUT
AccessionPrimary (citable) accession number: Q1R7T6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 44 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families