Reviewed, UniProtKB/Swiss-Prot P92979 (APR1_ARATH)

Names and origin

Protein names

Recommended name:
    5'-adenylylsulfate reductase 1, chloroplastic
    EC=1.8.4.9
Alternative name(s):
    Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 1
      Short name=APS sulfotransferase 1
    Thioredoxin-independent APS reductase 1
    3'-phosphoadenosine-5'-phosphosulfate reductase homolog 19
      Short name=PAPS reductase homolog 19
      Short name=Prh-19

Gene names

Name:	APR1
Synonyms:	PRH19
Ordered Locus Names:	At4g04610
ORF Names:	F4H6.13

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	465 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.
Catalytic activity	AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione.
Enzyme regulation	Stimulated by sodium sulfate > ammonium sulfate and is sensitive to inactivation by 5'AMP.
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. Ref.6
Sequence similarities	Belongs to the APS reductase family. Contains 1 thioredoxin domain.
Biophysicochemical properties	pH dependence: Optimum pH is 8.5.
Sequence caution	The sequence AAC49573.1 differs from that shown. Reason: Frameshift at position 453.

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 Ref.6 Inferred from direct assay. Source: TAIR sulfate reduction Ref.2 Inferred from direct assay. 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 Ref.6 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 – 53	53	Chloroplast Potential
	Chain	54 – 465	412	5'-adenylylsulfate reductase 1, chloroplastic		PRO_0000023214
Regions
	Domain	344 – 465	122	Thioredoxin
	Region	73 – 327	255	Reductase domain
Amino acid modifications
	Disulfide bond	385 ↔ 388		Redox-active By similarity
Experimental info
	Sequence conflict	86	1	E → D in AAC49573. Ref.2
	Sequence conflict	249 – 253	5	LDGGV → WMVEF in AAC49573. Ref.2
	Sequence conflict	371	1	N → F in AAC49561. Ref.1
	Sequence conflict	392	1	Missing in AAC49573. Ref.2
	Sequence conflict	400	1	D → A in AAC49561. Ref.1
	Sequence conflict	407	1	I → D in AAC49561. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P92979-1 [UniParc]. Last modified October 19, 2002. Version 2. Checksum: 7638DE9D9E4209CE	FASTA	465	51,714
	10 20 30 40 50 60 MAMSVNVSSS SSSGIINSRF GVSLEPKVSQ IGSLRLLDRV HVAPVSLNLS GKRSSSVKPL 70 80 90 100 110 120 NAEPKTKDSM IPLAATMVAE IAEEVEVVEI EDFEELAKKL ENASPLEIMD KALEKYGNDI 130 140 150 160 170 180 AIAFSGAEDV ALIEYAHLTG RPFRVFSLDT GRLNPETYRF FDAVEKHYGI RIEYMFPDSV 190 200 210 220 230 240 EVQGLVRSKG LFSFYEDGHQ ECCRVRKVRP LRRALKGLKA WITGQRKDQS PGTRSEIPVV 250 260 270 280 290 300 QVDPVFEGLD GGVGSLVKWN PVANVEGNDV WNFLRTMDVP VNTLHAAGYI SIGCEPCTKA 310 320 330 340 350 360 VLPGQHEREG RWWWEDAKAK ECGLHKGNVK ENSDDAKVNG ESKSAVADIF KSENLVTLSR 370 380 390 400 410 420 QGIENLMKLE NRKEPWIVVL YAPWCPFCQA MEASYDELAD KLAGSGIKVA KFRADGDQKE 430 440 450 460 FAKQELQLGS FPTILVFPKN SSRPIKYPSE KRDVESLTSF LNLVR

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.
[6]	"Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase." Bick J.-A., Aaslund F., Chen Y.C., Leustek T. Proc. Natl. Acad. Sci. U.S.A. 95:8404-8409(1998) [PubMed: 9653199] [Abstract] Cited for: CHARACTERIZATION OF DOMAINS. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U53864 mRNA. Translation: AAC49561.1. U43412 mRNA. Translation: AAC49573.1. Frameshift. AF016282 Genomic DNA. Translation: AAC26979.1. AF074021 Genomic DNA. Translation: AAD29775.1. AL161501 Genomic DNA. Translation: CAB80826.1. AF424582 mRNA. Translation: AAL11576.1. BT002612 mRNA. Translation: AAO11528.1.
IPI	IPI00538168.
PIR	B85058.
RefSeq	NP_192370.1.
UniGene	At.59149
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P92979.
Genome annotation databases
GeneID	825793.
GenomeReviews	Gene locus AT4G04610 in contig CT486007_GR.
KEGG	ath:AT4G04610.
NMPDR	fig|3702.1.peg.18268.
Organism-specific databases
TAIR	At4g04610.
Phylogenomic databases
OMA	P92979. RANTSAV.
Enzyme and pathway databases
BRENDA	1.8.4.9. 302.
Gene expression databases
ArrayExpress	P92979.
GermOnline	AT4G04610. 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

APR1_ARATH

Accession

Primary (citable) accession number: P92979
Secondary accession number(s): O48886, Q39248

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)