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Reviewed, UniProtKB/Swiss-Prot P92980 (APR3_ARATH)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    5'-adenylylsulfate reductase 3, chloroplastic
    EC=1.8.4.9
Alternative name(s):
    Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 3
      Short name=APS sulfotransferase 3
    Thioredoxin-independent APS reductase 3
    3'-phosphoadenosine-5'-phosphosulfate reductase homolog 26
      Short name=PAPS reductase homolog 26
      Short name=Prh-26
Gene names
Name: APR3
Synonyms: PRH26
Ordered Locus Names: At4g21990
ORF Names: F1N20.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.

Catalytic activity

AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione.

Enzyme regulation

Stimulated by sodium sulfate > ammonium sulfate By similarity.

Subcellular location

Plastidchloroplast Potential.

Tissue specificity

Leaves, roots and stem.

Induction

By sulfate starvation.

Domain

The C-terminal domain may function as glutaredoxin and mediates the interaction of the enzyme with glutathione (GSH). Active in GSH-dependent reduction of hydroxyethyldisulfide, cystine, dehydroascorbate, insulin disulfides and ribonucleotide reductase By similarity.

Sequence similarities

Belongs to the APS reductase family.

Contains 1 thioredoxin domain.

Sequence caution

The sequence AAC26978.1 differs from that shown. Reason: Frameshift at position 409.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6969Chloroplast Potential
Chain70 – 4583895'-adenylylsulfate reductase 3, chloroplastic
PRO_0000023216

Regions

Domain337 – 458122Thioredoxin
Region70 – 319250Reductase domain
Compositional bias8 – 5447Ser-rich

Amino acid modifications

Disulfide bond378 ↔ 381Redox-active By similarity

Experimental info

Sequence conflict281T → A in AAC26978. Ref.2
Sequence conflict1211D → Y in AAC26978. Ref.2
Sequence conflict3751A → R in AAC49562. Ref.1
Sequence conflict4361R → I in AAC49562. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P92980-1 [UniParc].

Last modified October 19, 2002. Version 2.
Checksum: E950C28E15F418CB

FASTA45850,695
        10         20         30         40         50         60 
MALAINVSSS SSSAISSSSF PSSDLKVTKI GSLRLLNRTN VSAASLSLSG KRSSVKALNV 

        70         80         90        100        110        120 
QSITKESIVA SEVTEKLDVV EVEDFEELAK RLENASPLEI MDKALEKFGN DIAIAFSGAE 

       130        140        150        160        170        180 
DVALIEYAHL TGRPYRVFSL DTGRLNPETY RLFDTVEKHY GIRIEYMFPD AVEVQALVRN 

       190        200        210        220        230        240 
KGLFSFYEDG HQECCRIRKV RPLRRALKGL RAWITGQRKD QSPGTRSEIP VVQVDPVFEG 

       250        260        270        280        290        300 
LDGGVGSLVK WNPVANVEGN DVWNFLRTMD VPVNTLHAAG YVSIGCEPCT RAVLPGQHER 

       310        320        330        340        350        360 
EGRWWWEDAK AKECGLHKGN IKENTNGNAT ANVNGTASVA DIFNSENVVN LSRQGIENLM 

       370        380        390        400        410        420 
KLENRKEAWI VVLYAPWCPF CQAMEASFDE LADKLGGSGV KVAKFRADGD QKDFAKKELQ 

       430        440        450 
LGSFPTILVF PKNSSRPIKY PSEKRDVDSL TSFLNLVR 

« Hide

References

« Hide 'large scale' references
[1]"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."
Gutierrez-Marcos J.F., Roberts M.A., Campbell E.I., Wray J.L.
Proc. Natl. Acad. Sci. U.S.A. 93:13377-13382(1996) [PubMed: 8917599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase."
Setya A., Murillo M., Leustek T.
Proc. Natl. Acad. Sci. U.S.A. 93:13383-13388(1996) [PubMed: 8917600] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: cv. Columbia.
[3]"Three genomic clones from Arabidopisis thaliana encoding 5'-adenylysulfate reductase."
Chen Y.C., Leustek T.
Plant Gene Register PGR98-030
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[4]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

U53865 mRNA. Translation: AAC49562.1.
U56922 mRNA. Translation: AAC26978.1. Frameshift.
AF016284 Genomic DNA. Translation: AAC26981.1.
AL022140 Genomic DNA. Translation: CAA18102.1.
AL161556 Genomic DNA. Translation: CAB79154.1.
AF428445 mRNA. Translation: AAL16214.1.
AY054175 mRNA. Translation: AAL06836.1.
AY062665 mRNA. Translation: AAL32743.1.
AY093319 mRNA. Translation: AAM13318.1.
AY103313 mRNA. Translation: AAM65364.1.
IPIIPI00545488.
PIRT49106.
RefSeqNP_193930.1.
UniGeneAt.2106

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEP92980.

Genome annotation databases

GeneID828288.
GenomeReviewsGene locus AT4G21990 in contig CT486007_GR.
KEGGath:AT4G21990.
NMPDRfig|3702.1.peg.20048.

Organism-specific databases

TAIRAt4g21990.

Phylogenomic databases

OMAP92980. NPVANVD.

Enzyme and pathway databases

BRENDA1.8.4.9. 302.

Gene expression databases

ArrayExpressP92980.
GermOnlineAT4G21990. Arabidopsis thaliana.

Family and domain databases

InterProIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004508. Thioredoxin-indep_APS_Rdtase.
IPR017936. Thioredoxin-like.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF01507. PAPS_reduct. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
TIGRFAMsTIGR00424. APS_reduc. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPR3_ARATH
AccessionPrimary (citable) accession number: P92980
Secondary accession number(s): O48887, Q38948
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents