Reviewed, UniProtKB/Swiss-Prot P92981 (APR2_ARATH)

Names and origin

Protein names

Recommended name:
    5'-adenylylsulfate reductase 2, chloroplastic
    EC=1.8.4.9
Alternative name(s):
    Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 2
      Short name=APS sulfotransferase 2
    Thioredoxin-independent APS reductase 2
    3'-phosphoadenosine-5'-phosphosulfate reductase homolog 43
      Short name=PAPS reductase homolog 43
      Short name=Prh-43

Gene names

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

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	454 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 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.

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, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Ref.1 Traceable author statement. 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 Ref.1 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 – 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
Amino acid modifications
	Disulfide bond	374 ↔ 377		Redox-active By similarity
Experimental info
	Sequence conflict	16	1	S → T in AAB57688. Ref.3
	Sequence conflict	16	1	S → T in AAM66987. Ref.7
	Sequence conflict	40	1	T → N in AAB57688. Ref.3
	Sequence conflict	40	1	T → N in AAM66987. Ref.7
	Sequence conflict	43	1	S → A in AAC49563. Ref.1
	Sequence conflict	45	1	R → G Ref.8
	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.7
	Sequence conflict	65	1	T → L in AAB57688. Ref.3
	Sequence conflict	65	1	T → L in AAM66987. Ref.7
	Sequence conflict	79	1	G → E in AAB57688. Ref.3
	Sequence conflict	79	1	G → E in AAM66987. Ref.7
	Sequence conflict	107	1	R → K in AAB57688. Ref.3
	Sequence conflict	107	1	R → K in AAM66987. Ref.7
	Sequence conflict	111	1	Q → E in AAB57688. Ref.3
	Sequence conflict	111	1	Q → E in AAM66987. Ref.7
	Sequence conflict	291	1	R → S in AAC26977. Ref.8
	Sequence conflict	322	1	K → F in AAC26977. Ref.8
	Sequence conflict	349	1	K → R in AAB57688. Ref.3
	Sequence conflict	349	1	K → R in AAM66987. Ref.7
	Sequence conflict	351	1	G → R in AAC26977. Ref.8
	Sequence conflict	385	1	I → V in AAB57688. Ref.3
	Sequence conflict	385	1	I → V in AAM66987. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P92981-1 [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]	"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]	"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].
[8]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. 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.
UniGene	At.25368
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P92981.
Genome annotation databases
GeneID	842514.
GenomeReviews	Gene locus AT1G62180 in contig CT485782_GR.
KEGG	ath:AT1G62180.
NMPDR	fig|3702.1.peg.5609.
Organism-specific databases
TAIR	At1g62180.
Enzyme and pathway databases
BRENDA	1.8.4.9. 302.
Gene expression databases
ArrayExpress	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. 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

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:	June 16, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)