P92980 (APR3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5'-adenylylsulfate reductase 3, chloroplastic
EC=1.8.4.9

Alternative name(s):
3'-phosphoadenosine-5'-phosphosulfate reductase homolog 26
Short name=PAPS reductase homolog 26
Short name=Prh-26
Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 3
Short name=APS sulfotransferase 3
Thioredoxin-independent APS reductase 3

Gene names

Name:	APR3
Synonyms:	PRH26
Ordered Locus Names:	At4g21990
ORF Names:	F1N20.90

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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.
Cofactor	Binds 1 4Fe-4S cluster By similarity.
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
Coding sequence diversity	Alternative splicing
Domain	Redox-active center Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Reference 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 response to stress Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation 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	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW adenylyl-sulfate reductase (glutathione) activity Inferred from electronic annotation. Source: EC adenylyl-sulfate reductase activity Inferred from direct assay. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P92980-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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
Sites
	Active site	378	1	Nucleophile By similarity
	Active site	381	1	Nucleophile By similarity
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	264	1	N → D in BAH57002. Ref.7
	Sequence conflict	338	1	S → T in AAM65133. Ref.8
	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)
	Isoform 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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"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.
[7]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed: 19423640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. Tissue: Rosette leaf.
[8]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. CP002687 Genomic DNA. Translation: AEE84539.1. 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. AK318887 mRNA. Translation: BAH57002.1. AY087591 mRNA. Translation: AAM65133.1.
IPI	IPI00545488.
PIR	T49106.
RefSeq	NP_193930.1. NM_118320.3.
UniGene	At.2106. At.24034.
3D structure databases
ProteinModelPortal	P92980.
SMR	P92980. Positions 83-307, 345-456.
ModBase	Search...
Protein-protein interaction databases
IntAct	P92980. 2 interactions.
STRING	P92980.
Proteomic databases
PRIDE	P92980.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G21990.1; AT4G21990.1; AT4G21990.
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
eggNOG	KOG0189.
HOGENOM	HBG758022.
InParanoid	P92980.
OMA	QECCRIR.
PhylomeDB	P92980.
ProtClustDB	PLN02309.
Gene expression databases
ArrayExpress	P92980.
Genevestigator	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. IPR012336. Thioredoxin-like_fold. IPR013766. Thioredoxin_domain. [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.
KO	K05907.
Pfam	PF01507. PAPS_reduct. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view]
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMs	TIGR00424. APS_reduc. 1 hit.
PROSITE	PS00194. THIOREDOXIN_1. False negative. 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): C0Z2S3 , O48887, Q38948, Q8LAV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 19, 2002
Last modified:	December 14, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program