APR1_ARATH
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 03-AUG-2022, entry version 169.
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; 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 Arabidopisis 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 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 [7]
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 [8]
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 [9]
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 [10]
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=AMP + glutathione disulfide + 2 H(+) + sulfite = 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};
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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; 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 PDBsum; 5YRY; -.
DR AlphaFoldDB; P92979; -.
DR SMR; P92979; -.
DR STRING; 3702.AT4G04610.1; -.
DR PaxDb; P92979; -.
DR PRIDE; P92979; -.
DR ProteomicsDB; 240602; -.
DR EnsemblPlants; AT4G04610.1; AT4G04610.1; AT4G04610.
DR GeneID; 825793; -.
DR Gramene; AT4G04610.1; AT4G04610.1; AT4G04610.
DR KEGG; ath:AT4G04610; -.
DR Araport; AT4G04610; -.
DR TAIR; locus:2125786; AT4G04610.
DR eggNOG; KOG0189; Eukaryota.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_044089_4_0_1; -.
DR OMA; MWNFLRA; -.
DR OrthoDB; 834258at2759; -.
DR PhylomeDB; P92979; -.
DR BioCyc; MetaCyc:AT4G04610-MON; -.
DR BRENDA; 1.8.4.9; 399.
DR PRO; PR:P92979; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P92979; baseline and differential.
DR Genevisible; P92979; AT.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IDA:TAIR.
DR GO; GO:0019419; P:sulfate reduction; IDA:TAIR.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00063; CysH; 1.
DR InterPro; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
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 Pfam; PF01507; PAPS_reduct; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00424; APS_reduc; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
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. 7; 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
