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A7ZQK5 (CYSH_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:EcE24377A_3064
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [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_1000057430

Sequences

Sequence LengthMass (Da)Tools
A7ZQK5 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: B8143A4DB84632BE

FASTA24427,973
        10         20         30         40         50         60 
MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV 

        70         80         90        100        110        120 
SLHLVNQIHP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL 

       130        140        150        160        170        180 
WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL 

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


LHEG 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV17378.1.
RefSeqYP_001464084.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZQK5.
SMRA7ZQK5. Positions 2-244.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZQK5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000018803; EBESCP00000017865; EBESCG00000017857.
GeneID5589881.
GenomeReviewsGene locus EcE24377A_3064 in contig CP000800_GR.
KEGGecw:EcE24377A_3064.
PATRIC18295444. VBIEscCol31211_3343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0175.
GeneTreeEBGT00050000009832.
HOGENOMHBG758022.
OMATNFRPYE.
ProtClustDBPRK02090.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_3064-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_ECO24
AccessionPrimary (citable) accession number: A7ZQK5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 33 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