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 P92981


[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 APR2_ARATH
Primary accession number P92981
Secondary accession numbers O04215 O04583 O22554 Q38947 Q541D4
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on October 19, 2002 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 79)
Name and origin of the protein
Protein name 5'-adenylylsulfate reductase 2, chloroplastic [Precursor]
Synonyms EC 1.8.4.9
Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 2
APS sulfotransferase 2
Thioredoxin-independent APS reductase 2
3'-phosphoadenosine-5'-phosphosulfate reductase homolog 43
PAPS reductase homolog 43
Prh-43
Gene name
Name: APR2
Synonyms: APSR, PRH43
OrderedLocusNames: At1g62180
ORFNames: F19K23.11
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1073/pnas.93.23.13377; PubMed=8917599 [NCBI, ExPASy, EBI, Israel, Japan]
Gutierrez-Marcos J.F., Roberts M.A., Campbell E.I., Wray J.L.;
"Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and 'APS reductase' activity.";
Proc. Natl. Acad. Sci. U.S.A. 93:13377-13382(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
TISSUE=Seedling;
Min B., Shin K.W., Ye X., Lee S.Y.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Gutierrez-Marcos J.F., Campbell E.I., Wray J.L.;
"A fourth member of the APS reductase gene family in Arabidopsis thaliana.";
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Chen Y.C., Leustek T.;
"Three genomic clones from Arabidopisis thaliana encoding 5'-adenylysulfate reductase.";
(er) Plant Gene Register PGR98-030.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 45-454.
STRAIN=cv. Columbia;
DOI=10.1073/pnas.93.23.13383; PubMed=8917600 [NCBI, ExPASy, EBI, Israel, Japan]
Setya A., Murillo M., Leustek T.;
"Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase.";
Proc. Natl. Acad. Sci. U.S.A. 93:13383-13388(1996).
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
U53866; AAC49563.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF023167; AAB80957.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U96045; AAB57688.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016283; AAC26980.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC000375; AAB60764.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360192; AAK25902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY040005; AAK64082.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088665; AAM66987.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U56921; AAC26977.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C96648; C96648.
RefSeq NP_176409.1; -.
UniGene At.25368
3D structure databases
ModBase P92981.
Organism-specific databases
TAIR At1g62180; -.
Gene expression databases
ArrayExpress P92981; -.
GermOnline AT1G62180; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0033741; Molecular function: adenylyl-sulfate reductase (glutathione) activity (inferred from electronic annotation from EC).
GO:0009973; Molecular function: adenylyl-sulfate reductase activity (inferred from direct assay from TAIR).
GO:0004604; Molecular function: phosphoadenylyl-sulfate reductase (thioredoxin) activity (inferred from direct assay from TAIR).
GO:0016740; Molecular function: transferase activity (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0019344; Biological process: cysteine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
GO:0019379; Biological process: sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) (traceable author statement from TAIR).
GO:0019421; Biological process: sulfate reduction, APS pathway (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004508; APS_reduc.
IPR002500; PAPS_reduct.
IPR014729; Rossmann-like_a/b/a_fold.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF01507; PAPS_reduct; 1.
PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.
PRINTS PR00421; THIOREDOXIN.
TIGRFAMs TIGR00424; APS_reduc; 1.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE P92981; -.
Genome annotation databases
GeneID 842514; -.
GenomeReviews CT485782_GR; AT1G62180.
KEGG ath:AT1G62180; -.
NMPDR fig|3702.1.peg.5609; -.
Other
ProtoNet P92981.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Chloroplast; Complete proteome; Cysteine biosynthesis; Oxidoreductase; Plastid; Redox-active center; Stress response; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    66  66     Chloroplast (Potential). 
CHAIN   67   454  388     5'-adenylylsulfate reductase 2, chloroplastic. PRO_0000023215
DOMAIN   333   454  122     Thioredoxin. 
REGION   67   319  253     Reductase domain. 
DISULFID   374   377        Redox-active (By similarity). 
CONFLICT   16    16        S -> T (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   40    40        T -> N (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   43    43        S -> A (in Ref. 1; AAC49563). 
CONFLICT   45    45        R -> G (in Ref. 8). 
CONFLICT   47    48        YS -> P (in Ref. 1; AAC49563). 
CONFLICT   57    58        HS -> SHT (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   65    65        T -> L (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   79    79        G -> E (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   107   107        R -> K (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   111   111        Q -> E (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   291   291        R -> S (in Ref. 8; AAC26977). 
CONFLICT   322   322        K -> F (in Ref. 8; AAC26977). 
CONFLICT   349   349        K -> R (in Ref. 3; AAB57688 and 7; AAM66987). 
CONFLICT   351   351        G -> R (in Ref. 8; AAC26977). 
CONFLICT   385   385        I -> V (in Ref. 3; AAB57688 and 7; AAM66987). 
Sequence information
Length: 454 AA [This is the length of the unprocessed precursor] Molecular weight: 50656 Da [This is the MW of the unprocessed precursor] CRC64: 4EB93C1FFC5E4636 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALAVTSSST AISGSSFSRS GASSESKALQ ICSIRLSDRT HLSQRRYSMK PLNAESHSRS 

        70         80         90        100        110        120 
ESWVTRASTL IAPEVEEKGG EVEDFEQLAK KLEDASPLEI MDKALERFGD QIAIAFSGAE 

       130        140        150        160        170        180 
DVALIEYARL TGKPFRVFSL DTGRLNPETY RLFDAVEKQY GIRIEYMFPD AVEVQALVRN 

       190        200        210        220        230        240 
KGLFSFYEDG HQECCRVRKV RPLRRALKGL KAWITGQRKD QSPGTRSEIP IVQVDPVFEG 

       250        260        270        280        290        300 
LDGGVGSLVK WNPLANVEGA DVWNFLRTMD VPVNALHAQG YVSIGCEPCT RPVLPGQHER 

       310        320        330        340        350        360 
EGRWWWEDAK AKECGLHKGN IKEEDGAADS KPAAVQEIFE SNNVVALSKG GVENLLKLEN 

       370        380        390        400        410        420 
RKEAWLVVLY APWCPFCQAM EASYIELAEK LAGKGVKVAK FRADGEQKEF AKQELQLGSF 

       430        440        450 
PTILLFPKRA PRAIKYPSEH RDVDSLMSFV NLLR 

P92981 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 au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!