ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8P607


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CYSH_XANCP
Primary accession number Q8P607
Secondary accession numbers None
Integrated into Swiss-Prot on March 25, 2003
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name Phosphoadenosine phosphosulfate reductase
Synonyms EC 1.8.4.8
PAPS reductase, thioredoxin dependent
PAdoPS reductase
3'-phosphoadenylylsulfate reductase
PAPS sulfotransferase
Gene name
Name: cysH
OrderedLocusNames: XCC3175
From
Xanthomonas campestris pv. campestris [TaxID: 340] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE012434; AAM42445.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_638521.1; -.
3D structure databases
HSSP P17854; 1SUR. [HSSP ENTRY / PDB]
ModBase Q8P607.
Enzyme and pathway databases
BioCyc XCAM190485:XCC3175-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004604; Molecular function: phosphoadenylyl-sulfate reductase (thioredoxin) activity (inferred from electronic annotation from HAMAP).
GO:0016740; Molecular function: transferase activity (inferred from electronic annotation from InterPro).
GO:0019344; Biological process: cysteine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019379; Biological process: sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00063; -; 1.
PBIL [Tree]
InterPro IPR004511; CysH.
IPR002500; PAPS_reduct.
IPR011800; PAPS_reductase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF01507; PAPS_reduct; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00434; cysH; 1.
TIGR02057; PAPS_reductase; 1.
Genome annotation databases
GeneID 999271; -.
GenomeReviews AE008922_GR; XCC3175.
KEGG xcc:XCC3175; -.
Phylogenomic databases
HOGENOM Q8P607; -.
Genome annotation databases
CMR Q8P607; XCC3175.
Other
ProtoNet Q8P607.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   241  241     Phosphoadenosine phosphosulfate reductase. PRO_0000100657
Sequence information
Length: 241 AA [This is the length of the unprocessed precursor] Molecular weight: 27637 Da [This is the MW of the unprocessed precursor] CRC64: 6CB195BA3A561C26 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTALPATSIA APSLDDLDAL NAHLETLRAD ERVAWALQHG PQQAALSSSF GAQSAVTLHL 

        70         80         90        100        110        120 
LTQQRPDIPV ILIDTGYLFP ETYRFADALT ERLSLNLQVY RPLVSRAWME ARHGRLWEQG 

       130        140        150        160        170        180 
MVGIDQYNNL RKVEPMRRAL DELNVGTWFT GLRRSQSGGR AQTPIVQKRG DRYKISPIAD 

       190        200        210        220        230        240 
WTDRDVWQYL QAHALPYHPL WEQGYVSIGD FHTTRRWEPG MREEDTRFFG LKRECGIHED 


I 

Q8P607 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!