Reviewed, UniProtKB/Swiss-Prot P92980 (APR3_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis Stress response
Cellular component	Chloroplast Plastid
Domain	Redox-active center Transit peptide
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation Ref.2 Inferred from direct assay. Source: TAIR sulfate reduction Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast Inferred from direct assay. Source: TAIR
Molecular function	adenylyl-sulfate reductase (glutathione) activity Inferred from electronic annotation. Source: EC adenylyl-sulfate reductase activity Inferred from direct assay. Source: TAIR transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 69	69	Chloroplast Potential
	Chain	70 – 458	389	5'-adenylylsulfate reductase 3, chloroplastic		PRO_0000023216
Regions
	Domain	337 – 458	122	Thioredoxin
	Region	70 – 319	250	Reductase domain
	Compositional bias	8 – 54	47	Ser-rich
Amino acid modifications
	Disulfide bond	378 ↔ 381		Redox-active By similarity
Experimental info
	Sequence conflict	28	1	T → A in AAC26978. Ref.2
	Sequence conflict	121	1	D → Y in AAC26978. Ref.2
	Sequence conflict	375	1	A → R in AAC49562. Ref.1
	Sequence conflict	436	1	R → I in AAC49562. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P92980-1 [UniParc]. Last modified October 19, 2002. Version 2. Checksum: E950C28E15F418CB	FASTA	458	50,695
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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
EMBLGenBankDDBJ	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.
IPI	IPI00545488.
PIR	T49106.
RefSeq	NP_193930.1.
UniGene	At.2106
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P92980.
Genome annotation databases
GeneID	828288.
GenomeReviews	Gene locus AT4G21990 in contig CT486007_GR.
KEGG	ath:AT4G21990.
NMPDR	fig|3702.1.peg.20048.
Organism-specific databases
TAIR	At4g21990.
Phylogenomic databases
OMA	P92980. NPVANVD.
Enzyme and pathway databases
BRENDA	1.8.4.9. 302.
Gene expression databases
ArrayExpress	P92980.
GermOnline	AT4G21990. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002500. 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]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF01507. PAPS_reduct. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view]
TIGRFAMs	TIGR00424. APS_reduc. 1 hit.
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APR3_ARATH

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)