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UniProtKB/Swiss-Prot entry Q81T49


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

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Entry information
Entry name CYSH_BACAN
Primary accession number Q81T49
Secondary accession numbers Q6I1D2 Q6KV78
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
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: BA_1440, GBAA1440, BAS1330
From
Bacillus anthracis [TaxID: 1392] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ames / isolate Porton;
DOI=10.1038/nature01586; PubMed=12721629 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.;
"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria.";
Nature 423:81-86(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ames ancestor;
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.;
"Bacillus anthracis comparative genomics.";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Sterne;
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.;
"Complete genome sequence of Bacillus anthracis Sterne.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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
AE016879; AAP25382.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017334; AAT30539.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017225; AAT53650.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_843896.1; -.
YP_018064.1; -.
YP_027599.1; -.
3D structure databases
HSSP P17854; 1SUR. [HSSP ENTRY / PDB]
ModBase Q81T49.
Enzyme and pathway databases
BioCyc BANT260799:BAS1330-MON; -.
BANT261594:GBAA1440-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 IPR011798; APS_reductase.
IPR004511; CysH.
IPR002500; PAPS_reduct.
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 TIGR02055; APS_reductase; 1.
TIGR00434; cysH; 1.
ProtoNet Q81T49.
Genome annotation databases
GeneID 1086013; -.
2816195; -.
2849690; -.
GenomeReviews AE016879_GR; BA_1440.
AE017225_GR; BAS1330.
AE017334_GR; GBAA1440.
KEGG ban:BA1440; -.
bar:GBAA1440; -.
bat:BAS1330; -.
TIGR BA_1440; -.
GBAA1440; -.
Phylogenomic databases
HOGENOM Q81T49; -.
Other
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   226  226     Phosphoadenosine phosphosulfate reductase. PRO_0000100623
Sequence information
Length: 226 AA [This is the length of the unprocessed precursor] Molecular weight: 26393 Da [This is the MW of the unprocessed precursor] CRC64: 3FF2A81C8BCA282A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLTYETWEEN ETKGALSVLS WAYKEYKSEI VYACSFGVEG MVLLDLINQV NPSAKVVFLD 

        70         80         90        100        110        120 
TNVHFQETYE LIQKVRERFP SLNIIEKQPK LTLDEQDKLH GDKLWESNPN LCCKIRKILP 

       130        140        150        160        170        180 
LEESLANEKA WISGLRREQS ETRKHTKFIN QDHRFQSIKV CPLIHWTWKE VWRYVYKHSL 

       190        200        210        220 
PYNSLHDIGY PSIGCEKCTL PVGEGGDSRD GRWAGKVKTE CGLHYQ 

Q81T49 in FASTA format

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