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Q1LTP3 (CYSH_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:BCI_0216
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length245 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 – 245245Phosphoadenosine phosphosulfate reductase HAMAP MF_00063
PRO_1000008919

Sequences

Sequence LengthMass (Da)Tools
Q1LTP3 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 1D8FCC91FFDEF631

FASTA24528,240
        10         20         30         40         50         60 
MKVLDLRELN AMDKSQQTEA MTTVNLQLEN MTAEHRVSWA LEHLPQPAVL SSSFGIQAAV 

        70         80         90        100        110        120 
SLHLVTSQQP NIPVILTDTG YLFPETYQFI DQLTEQLKLN LKVFRAYISP AWQEARYGKL 

       130        140        150        160        170        180 
WEQGIKGIQL YNKINKVEPM NRALIQLGSL TWFAGLRRTQ SSSRSKLPVL AVQQCLFKLL 

       190        200        210        220        230        240 
PIIDWDNRQV HSYLKKHGLN YHPLWEQGYL SVGDTHTTCK WTPGMNEEDT RFFGLKRECG 


IHEEK 

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References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF14272.1.
RefSeqYP_588671.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTP3.
SMRQ1LTP3. Positions 4-243.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LTP3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056286.
GenomeReviewsGene locus BCI_0216 in contig CP000238_GR.
KEGGbci:BCI_0216.
PATRIC21073931. VBIBauCic75062_0204.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0175.
HOGENOMHBG758022.
OMAAIHGTRF.
PhylomeDBQ1LTP3.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0216-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_BAUCH
AccessionPrimary (citable) accession number: Q1LTP3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 41 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