P92981 (APR2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5'-adenylylsulfate reductase 2, chloroplastic
EC=1.8.4.9

Alternative name(s):
3'-phosphoadenosine-5'-phosphosulfate reductase homolog 43
Short name=PAPS reductase homolog 43
Short name=Prh-43
Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 2
Short name=APS sulfotransferase 2
Thioredoxin-independent APS reductase 2

Gene names

Name:	APR2
Synonyms:	APSR, PRH43
Ordered Locus Names:	At1g62180
ORF Names:	F19K23.11

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	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. Ref.10
Catalytic activity	AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione.
Cofactor	Binds 1 4Fe-4S cluster. Ref.10
Enzyme regulation	Stimulated by sodium sulfate > ammonium sulfate By similarity.
Subcellular location	Plastid › chloroplast Potential.
Tissue specificity	Leaves 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 AAC26977.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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
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, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Traceable author statement Ref.1. Source: TAIR
Cellular component	chloroplast stroma 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 phosphoadenylyl-sulfate reductase (thioredoxin) activity Inferred from direct assay Ref.1. Source: TAIR
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: P92981-1)

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 – 66	66	Chloroplast Potential
	Chain	67 – 454	388	5'-adenylylsulfate reductase 2, chloroplastic		PRO_0000023215
Regions
	Domain	333 – 454	122	Thioredoxin
	Region	67 – 319	253	Reductase domain
Sites
	Active site	374	1	Nucleophile By similarity
	Active site	377	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	374 ↔ 377		Redox-active By similarity
Experimental info
	Mutagenesis	195	1	C → S: Slightly reduces activity. Ref.10
	Mutagenesis	314	1	C → S: Abolishes activity. Ref.10
	Sequence conflict	16	1	S → T in AAB57688. Ref.3
	Sequence conflict	16	1	S → T in AAM66987. Ref.8
	Sequence conflict	40	1	T → N in AAB57688. Ref.3
	Sequence conflict	40	1	T → N in AAM66987. Ref.8
	Sequence conflict	43	1	S → A in AAC49563. Ref.1
	Sequence conflict	47 – 48	2	YS → P in AAC49563. Ref.1
	Sequence conflict	57 – 58	2	HS → SHT in AAB57688. Ref.3
	Sequence conflict	57 – 58	2	HS → SHT in AAM66987. Ref.8
	Sequence conflict	65	1	T → L in AAB57688. Ref.3
	Sequence conflict	65	1	T → L in AAM66987. Ref.8
	Sequence conflict	79	1	G → E in AAB57688. Ref.3
	Sequence conflict	79	1	G → E in AAM66987. Ref.8
	Sequence conflict	107	1	R → K in AAB57688. Ref.3
	Sequence conflict	107	1	R → K in AAM66987. Ref.8
	Sequence conflict	111	1	Q → E in AAB57688. Ref.3
	Sequence conflict	111	1	Q → E in AAM66987. Ref.8
	Sequence conflict	291	1	R → S in AAC26977. Ref.9
	Sequence conflict	322	1	K → F in AAC26977. Ref.9
	Sequence conflict	349	1	K → R in AAB57688. Ref.3
	Sequence conflict	349	1	K → R in AAM66987. Ref.8
	Sequence conflict	351	1	G → R in AAC26977. Ref.9
	Sequence conflict	385	1	I → V in AAB57688. Ref.3
	Sequence conflict	385	1	I → V in AAM66987. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 19, 2002. Version 2. Checksum: 4EB93C1FFC5E4636	FASTA	454	50,656
	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

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]	Min B., Shin K.W., Ye X., Lee S.Y. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Seedling.
[3]	"A fourth member of the APS reductase gene family in Arabidopsis thaliana." Gutierrez-Marcos J.F., Campbell E.I., Wray J.L. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[7]	"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.
[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].
[9]	"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] OF 45-454. Strain: cv. Columbia.
[10]	"Plant adenosine 5'-phosphosulfate reductase is a novel iron-sulfur protein." Kopriva S., Buechert T., Fritz G., Suter M., Weber M., Benda R., Schaller J., Feller U., Schuermann P., Schuenemann V., Trautwein A.X., Kroneck P.M., Brunold C. J. Biol. Chem. 276:42881-42886(2001) [PubMed: 11553635] [Abstract] Cited for: FUNCTION, COFACTOR, MUTAGENESIS OF CYS-195 AND CYS-314.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U53866 mRNA. Translation: AAC49563.1. AF023167 mRNA. Translation: AAB80957.1. U96045 mRNA. Translation: AAB57688.1. AF016283 Genomic DNA. Translation: AAC26980.1. AC000375 Genomic DNA. Translation: AAB60764.1. CP002684 Genomic DNA. Translation: AEE33931.1. AF360192 mRNA. Translation: AAK25902.1. AY040005 mRNA. Translation: AAK64082.1. AY088665 mRNA. Translation: AAM66987.1. U56921 mRNA. Translation: AAC26977.1. Different initiation.
IPI	IPI00546874.
PIR	C96648.
RefSeq	NP_176409.1. NM_104899.2.
UniGene	At.25368. At.74995.
3D structure databases
ProteinModelPortal	P92981.
SMR	P92981. Positions 83-307, 342-453.
ModBase	Search...
Protein-protein interaction databases
IntAct	P92981. 1 interaction.
STRING	P92981.
Proteomic databases
PRIDE	P92981.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G62180.1; AT1G62180.1; AT1G62180.
GeneID	842514.
GenomeReviews	Gene locus AT1G62180 in contig CT485782_GR.
KEGG	ath:AT1G62180.
NMPDR	fig|3702.1.peg.5609.
Organism-specific databases
TAIR	At1g62180.
Phylogenomic databases
eggNOG	KOG0189.
HOGENOM	HBG758022.
InParanoid	P92981.
OMA	MEASYIE.
PhylomeDB	P92981.
ProtClustDB	PLN02309.
Gene expression databases
ArrayExpress	P92981.
Genevestigator	P92981.
GermOnline	AT1G62180. 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

APR2_ARATH

Accession

Primary (citable) accession number: P92981
Secondary accession number(s): O04215 , O04583, O22554, Q38947, Q541D4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 19, 2002
Last modified:	December 14, 2011
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program