ID APR1_ARATH Reviewed; 465 AA. AC P92979; O48886; Q39248; Q56ZY2; Q8LA60; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 2. DT 02-SEP-2026, entry version 187. DE RecName: Full=5'-adenylylsulfate reductase 1, chloroplastic; DE EC=1.8.4.9; DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate reductase homolog 19; DE Short=PAPS reductase homolog 19; DE Short=Prh-19; DE AltName: Full=Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 1; DE Short=APS sulfotransferase 1; DE AltName: Full=Thioredoxin-independent APS reductase 1; DE Flags: Precursor; GN Name=APR1; Synonyms=PRH19; OrderedLocusNames=At4g04610; GN ORFNames=F4H6.13; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION. RC STRAIN=cv. Columbia; RX PubMed=8917599; DOI=10.1073/pnas.93.23.13377; RA Gutierrez-Marcos J.F., Roberts M.A., Campbell E.I., Wray J.L.; RT "Three members of a novel small gene-family from Arabidopsis thaliana able RT to complement functionally an Escherichia coli mutant defective in PAPS RT reductase activity encode proteins with a thioredoxin-like domain and 'APS RT reductase' activity."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13377-13382(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=cv. Columbia; RX PubMed=8917600; DOI=10.1073/pnas.93.23.13383; RA Setya A., Murillo M., Leustek T.; RT "Sulfate reduction in higher plants: molecular evidence for a novel 5'- RT adenylylsulfate reductase."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13383-13388(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; RA Chen Y.C., Leustek T.; RT "Three genomic clones from Arabidopsis thaliana encoding 5'-adenylysulfate RT reductase."; RL (er) Plant Gene Register PGR98-030(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [6] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-465. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP CHARACTERIZATION OF DOMAINS. RC STRAIN=cv. Columbia; RX PubMed=9653199; DOI=10.1073/pnas.95.14.8404; RA Bick J.-A., Aaslund F., Chen Y.C., Leustek T.; RT "Glutaredoxin function for the carboxyl-terminal domain of the plant-type RT 5'-adenylylsulfate reductase."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8404-8409(1998). RN [11] RP INDUCTION BY CADMIUM. RC STRAIN=cv. Columbia; RX PubMed=16502469; DOI=10.1002/pmic.200500543; RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V., RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C., RA Ezan E., Garin J., Bourguignon J.; RT "The early responses of Arabidopsis thaliana cells to cadmium exposure RT explored by protein and metabolite profiling analyses."; RL Proteomics 6:2180-2198(2006). CC -!- FUNCTION: Reduces sulfate for Cys biosynthesis. Substrate preference is CC adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'- CC phosphosulfate (PAPS). Uses glutathione or DTT as source of protons. CC -!- CATALYTIC ACTIVITY: CC Reaction=glutathione disulfide + sulfite + AMP + 2 H(+) = adenosine 5'- CC phosphosulfate + 2 glutathione; Xref=Rhea:RHEA:14141, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:58243, ChEBI:CHEBI:58297, ChEBI:CHEBI:456215; EC=1.8.4.9; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Stimulated by sodium sulfate > ammonium sulfate CC and is sensitive to inactivation by 5'AMP. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.5.; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Leaves, roots and stem. CC -!- INDUCTION: Induced by sulfate starvation (PubMed:8917599). Induced by CC cadmium (PubMed:16502469). {ECO:0000269|PubMed:16502469, CC ECO:0000269|PubMed:8917599}. CC -!- DOMAIN: The C-terminal domain may function as glutaredoxin and mediates CC the interaction of the enzyme with glutathione (GSH). Active in GSH- CC dependent reduction of hydroxyethyldisulfide, cystine, CC dehydroascorbate, insulin disulfides and ribonucleotide reductase. CC -!- SIMILARITY: Belongs to the APS reductase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC49573.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U53864; AAC49561.1; -; mRNA. DR EMBL; U43412; AAC49573.1; ALT_FRAME; mRNA. DR EMBL; AF016282; AAC26979.1; -; Genomic_DNA. DR EMBL; AF074021; AAD29775.1; -; Genomic_DNA. DR EMBL; AL161501; CAB80826.1; -; Genomic_DNA. DR EMBL; CP002687; AEE82402.1; -; Genomic_DNA. DR EMBL; OZ408686; CAO7046145.1; -; Genomic_DNA. DR EMBL; AF424582; AAL11576.1; -; mRNA. DR EMBL; BT002612; AAO11528.1; -; mRNA. DR EMBL; AY088011; AAM65557.1; -; mRNA. DR EMBL; AK220828; BAD94133.1; -; mRNA. DR PIR; B85058; B85058. DR RefSeq; NP_192370.1; NM_116699.3. DR PDB; 5YRY; X-ray; 2.70 A; A=353-461. DR AlphaFoldDB; P92979; -. DR SMR; P92979; -. DR FunCoup; P92979; 146. DR STRING; 3702.P92979; -. DR PaxDb; 3702-P92979; -. DR ProteomicsDB; 240602; -. DR GeneID; 825793; -. DR KEGG; ath:AT4G04610; -. DR Araport; AT4G04610; -. DR TAIR; AT4G04610; APR1. DR eggNOG; KOG0189; Eukaryota. DR eggNOG; KOG0191; Eukaryota. DR HOGENOM; CLU_044089_4_0_1; -. DR InParanoid; P92979; -. DR OMA; MAMSVNV; -. DR OrthoDB; 7869097at2759; -. DR PhylomeDB; P92979; -. DR BioCyc; MetaCyc:AT4G04610-MONOMER; -. DR BRENDA; 1.8.4.9; 399. DR PRO; PR:P92979; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; P92979; baseline and differential. DR GO; GO:0009507; C:chloroplast; ISS:TAIR. DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR. DR GO; GO:0009536; C:plastid; TAS:TAIR. DR GO; GO:0033741; F:adenylyl-sulfate reductase (glutathione) activity; IEA:UniProtKB-EC. DR GO; GO:0009973; F:adenylyl-sulfate reductase activity; IDA:TAIR. DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:InterPro. DR GO; GO:0000103; P:sulfate assimilation; IDA:TAIR. DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro. DR CDD; cd23945; PAPS_reductase; 1. DR CDD; cd02993; PDI_a_APS_reductase; 1. DR FunFam; 3.40.50.620:FF:000153; Phosphoadenosine phosphosulfate reductase; 1. DR FunFam; 3.40.30.10:FF:000252; Phosphoadenosine-phosphosulphate reductase; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00063; CysH; 1. DR InterPro; IPR004511; PAPS/APS_Rdtase. DR InterPro; IPR002500; PAPS_reduct_dom. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004508; Thioredoxin-indep_APS_Rdtase. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR00424; APS_reduc; 1. DR NCBIfam; NF002537; PRK02090.1; 1. DR PANTHER; PTHR46482:SF9; 5'-ADENYLYLSULFATE REDUCTASE 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR46482; 5'-ADENYLYLSULFATE REDUCTASE 3, CHLOROPLASTIC; 1. DR Pfam; PF01507; PAPS_reduct; 1. DR Pfam; PF00085; Thioredoxin; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. DR PDBsum; 5YRY; -. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Amino-acid biosynthesis; Chloroplast; KW Cysteine biosynthesis; Disulfide bond; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Plastid; Redox-active center; Reference proteome; KW Stress response; Transit peptide. FT TRANSIT 1..53 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 54..465 FT /note="5'-adenylylsulfate reductase 1, chloroplastic" FT /id="PRO_0000023214" FT DOMAIN 344..465 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT REGION 73..327 FT /note="Reductase domain" FT ACT_SITE 385 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 388 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT DISULFID 385..388 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT CONFLICT 67 FT /note="K -> N (in Ref. 8; AAM65557)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="E -> D (in Ref. 2; AAC49573)" FT /evidence="ECO:0000305" FT CONFLICT 249..253 FT /note="LDGGV -> WMVEF (in Ref. 2; AAC49573)" FT /evidence="ECO:0000305" FT CONFLICT 371 FT /note="N -> F (in Ref. 1; AAC49561)" FT /evidence="ECO:0000305" FT CONFLICT 392 FT /note="Missing (in Ref. 2; AAC49573)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="D -> A (in Ref. 1; AAC49561)" FT /evidence="ECO:0000305" FT CONFLICT 407 FT /note="I -> D (in Ref. 1; AAC49561)" FT /evidence="ECO:0000305" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:5YRY" FT HELIX 360..368 FT /evidence="ECO:0007829|PDB:5YRY" FT STRAND 376..381 FT /evidence="ECO:0007829|PDB:5YRY" FT HELIX 386..402 FT /evidence="ECO:0007829|PDB:5YRY" FT STRAND 408..413 FT /evidence="ECO:0007829|PDB:5YRY" FT HELIX 418..425 FT /evidence="ECO:0007829|PDB:5YRY" FT STRAND 430..437 FT /evidence="ECO:0007829|PDB:5YRY" FT STRAND 445..447 FT /evidence="ECO:0007829|PDB:5YRY" FT HELIX 451..461 FT /evidence="ECO:0007829|PDB:5YRY" SQ SEQUENCE 465 AA; 51714 MW; 7638DE9D9E4209CE CRC64; MAMSVNVSSS SSSGIINSRF GVSLEPKVSQ IGSLRLLDRV HVAPVSLNLS GKRSSSVKPL NAEPKTKDSM IPLAATMVAE IAEEVEVVEI EDFEELAKKL ENASPLEIMD KALEKYGNDI AIAFSGAEDV ALIEYAHLTG RPFRVFSLDT GRLNPETYRF FDAVEKHYGI RIEYMFPDSV EVQGLVRSKG LFSFYEDGHQ ECCRVRKVRP LRRALKGLKA WITGQRKDQS PGTRSEIPVV QVDPVFEGLD GGVGSLVKWN PVANVEGNDV WNFLRTMDVP VNTLHAAGYI SIGCEPCTKA VLPGQHEREG RWWWEDAKAK ECGLHKGNVK ENSDDAKVNG ESKSAVADIF KSENLVTLSR QGIENLMKLE NRKEPWIVVL YAPWCPFCQA MEASYDELAD KLAGSGIKVA KFRADGDQKE FAKQELQLGS FPTILVFPKN SSRPIKYPSE KRDVESLTSF LNLVR //