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Protein

5'-adenylylsulfate reductase 1, chloroplastic

Gene

APR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Enzyme regulationi

Stimulated by sodium sulfate > ammonium sulfate and is sensitive to inactivation by 5'AMP.

pH dependencei

Optimum pH is 8.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei385 – 3851NucleophileBy similarity
Active sitei388 – 3881NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cysteine biosynthetic process Source: UniProtKB-KW
  • sulfate assimilation Source: TAIR
  • sulfate reduction Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis, Stress response

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:AT4G04610-MONOMER.
BRENDAi1.8.4.9. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-adenylylsulfate reductase 1, chloroplastic (EC:1.8.4.9)
Alternative name(s):
3'-phosphoadenosine-5'-phosphosulfate reductase homolog 19
Short name:
PAPS reductase homolog 19
Short name:
Prh-19
Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 1
Short name:
APS sulfotransferase 1
Thioredoxin-independent APS reductase 1
Gene namesi
Name:APR1
Synonyms:PRH19
Ordered Locus Names:At4g04610
ORF Names:F4H6.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G04610.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353ChloroplastSequence analysisAdd
BLAST
Chaini54 – 4654125'-adenylylsulfate reductase 1, chloroplasticPRO_0000023214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi385 ↔ 388Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP92979.
PRIDEiP92979.

Expressioni

Tissue specificityi

Leaves, roots and stem.

Inductioni

By sulfate starvation.

Gene expression databases

GenevisibleiP92979. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G04610.1.

Structurei

3D structure databases

ProteinModelPortaliP92979.
SMRiP92979. Positions 92-315, 352-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini344 – 465122ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 327255Reductase domainAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the APS reductase family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0189. Eukaryota.
KOG0191. Eukaryota.
COG0175. LUCA.
HOGENOMiHOG000242337.
KOiK05907.
OMAiPKVSQIG.
PhylomeDBiP92979.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004508. Thioredoxin-indep_APS_Rdtase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00424. APS_reduc. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P92979-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMSVNVSSS SSSGIINSRF GVSLEPKVSQ IGSLRLLDRV HVAPVSLNLS
60 70 80 90 100
GKRSSSVKPL NAEPKTKDSM IPLAATMVAE IAEEVEVVEI EDFEELAKKL
110 120 130 140 150
ENASPLEIMD KALEKYGNDI AIAFSGAEDV ALIEYAHLTG RPFRVFSLDT
160 170 180 190 200
GRLNPETYRF FDAVEKHYGI RIEYMFPDSV EVQGLVRSKG LFSFYEDGHQ
210 220 230 240 250
ECCRVRKVRP LRRALKGLKA WITGQRKDQS PGTRSEIPVV QVDPVFEGLD
260 270 280 290 300
GGVGSLVKWN PVANVEGNDV WNFLRTMDVP VNTLHAAGYI SIGCEPCTKA
310 320 330 340 350
VLPGQHEREG RWWWEDAKAK ECGLHKGNVK ENSDDAKVNG ESKSAVADIF
360 370 380 390 400
KSENLVTLSR QGIENLMKLE NRKEPWIVVL YAPWCPFCQA MEASYDELAD
410 420 430 440 450
KLAGSGIKVA KFRADGDQKE FAKQELQLGS FPTILVFPKN SSRPIKYPSE
460
KRDVESLTSF LNLVR
Length:465
Mass (Da):51,714
Last modified:October 19, 2002 - v2
Checksum:i7638DE9D9E4209CE
GO

Sequence cautioni

The sequence AAC49573.1 differs from that shown. Reason: Frameshift at position 453. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671K → N in AAM65557 (Ref. 7) Curated
Sequence conflicti86 – 861E → D in AAC49573 (PubMed:8917600).Curated
Sequence conflicti249 – 2535LDGGV → WMVEF in AAC49573 (PubMed:8917600).Curated
Sequence conflicti371 – 3711N → F in AAC49561 (PubMed:8917599).Curated
Sequence conflicti392 – 3921Missing in AAC49573 (PubMed:8917600).Curated
Sequence conflicti400 – 4001D → A in AAC49561 (PubMed:8917599).Curated
Sequence conflicti407 – 4071I → D in AAC49561 (PubMed:8917599).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CP002687 Genomic DNA. Translation: AEE82402.1.
AF424582 mRNA. Translation: AAL11576.1.
BT002612 mRNA. Translation: AAO11528.1.
AY088011 mRNA. Translation: AAM65557.1.
AK220828 mRNA. Translation: BAD94133.1.
PIRiB85058.
RefSeqiNP_192370.1. NM_116699.2.
UniGeneiAt.47507.
At.59149.

Genome annotation databases

EnsemblPlantsiAT4G04610.1; AT4G04610.1; AT4G04610.
GeneIDi825793.
GrameneiAT4G04610.1; AT4G04610.1; AT4G04610.
KEGGiath:AT4G04610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CP002687 Genomic DNA. Translation: AEE82402.1.
AF424582 mRNA. Translation: AAL11576.1.
BT002612 mRNA. Translation: AAO11528.1.
AY088011 mRNA. Translation: AAM65557.1.
AK220828 mRNA. Translation: BAD94133.1.
PIRiB85058.
RefSeqiNP_192370.1. NM_116699.2.
UniGeneiAt.47507.
At.59149.

3D structure databases

ProteinModelPortaliP92979.
SMRiP92979. Positions 92-315, 352-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G04610.1.

Proteomic databases

PaxDbiP92979.
PRIDEiP92979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G04610.1; AT4G04610.1; AT4G04610.
GeneIDi825793.
GrameneiAT4G04610.1; AT4G04610.1; AT4G04610.
KEGGiath:AT4G04610.

Organism-specific databases

TAIRiAT4G04610.

Phylogenomic databases

eggNOGiKOG0189. Eukaryota.
KOG0191. Eukaryota.
COG0175. LUCA.
HOGENOMiHOG000242337.
KOiK05907.
OMAiPKVSQIG.
PhylomeDBiP92979.

Enzyme and pathway databases

BioCyciMetaCyc:AT4G04610-MONOMER.
BRENDAi1.8.4.9. 399.

Miscellaneous databases

PROiP92979.

Gene expression databases

GenevisibleiP92979. AT.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004508. Thioredoxin-indep_APS_Rdtase.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00424. APS_reduc. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-465.
    Strain: cv. Columbia.
  9. "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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF DOMAINS.
    Strain: cv. Columbia.

Entry informationi

Entry nameiAPR1_ARATH
AccessioniPrimary (citable) accession number: P92979
Secondary accession number(s): O48886
, Q39248, Q56ZY2, Q8LA60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: February 17, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.