APR3_ARATH
ID APR3_ARATH Reviewed; 458 AA.
AC P92980; C0Z2S3; O48887; Q38948; Q8LAV2;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=5'-adenylylsulfate reductase 3, chloroplastic;
DE EC=1.8.4.9;
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate reductase homolog 26;
DE Short=PAPS reductase homolog 26;
DE Short=Prh-26;
DE AltName: Full=Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 3;
DE Short=APS sulfotransferase 3;
DE AltName: Full=Thioredoxin-independent APS reductase 3;
DE Flags: Precursor;
GN Name=APR3; Synonyms=PRH26; OrderedLocusNames=At4g21990; ORFNames=F1N20.90;
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].
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].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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.
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 {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P92980-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Leaves, roots and stem.
CC -!- INDUCTION: By sulfate starvation.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APS reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC26978.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U53865; AAC49562.1; -; mRNA.
DR EMBL; U56922; AAC26978.1; ALT_FRAME; mRNA.
DR EMBL; AF016284; AAC26981.1; -; Genomic_DNA.
DR EMBL; AL022140; CAA18102.1; -; Genomic_DNA.
DR EMBL; AL161556; CAB79154.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84539.1; -; Genomic_DNA.
DR EMBL; AF428445; AAL16214.1; -; mRNA.
DR EMBL; AY054175; AAL06836.1; -; mRNA.
DR EMBL; AY062665; AAL32743.1; -; mRNA.
DR EMBL; AY093319; AAM13318.1; -; mRNA.
DR EMBL; AY103313; AAM65364.1; -; mRNA.
DR EMBL; AK318887; BAH57002.1; -; mRNA.
DR EMBL; AY087591; AAM65133.1; -; mRNA.
DR PIR; T49106; T49106.
DR RefSeq; NP_193930.1; NM_118320.3. [P92980-1]
DR AlphaFoldDB; P92980; -.
DR SMR; P92980; -.
DR BioGRID; 13577; 1.
DR IntAct; P92980; 2.
DR STRING; 3702.AT4G21990.1; -.
DR PaxDb; P92980; -.
DR PRIDE; P92980; -.
DR ProteomicsDB; 244440; -. [P92980-1]
DR EnsemblPlants; AT4G21990.1; AT4G21990.1; AT4G21990. [P92980-1]
DR GeneID; 828288; -.
DR Gramene; AT4G21990.1; AT4G21990.1; AT4G21990. [P92980-1]
DR KEGG; ath:AT4G21990; -.
DR Araport; AT4G21990; -.
DR TAIR; locus:2120628; AT4G21990.
DR eggNOG; KOG0189; Eukaryota.
DR eggNOG; KOG0191; Eukaryota.
DR OrthoDB; 834258at2759; -.
DR PhylomeDB; P92980; -.
DR BioCyc; MetaCyc:AT4G21990-MON; -.
DR PRO; PR:P92980; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P92980; baseline and differential.
DR Genevisible; P92980; AT.
DR GO; GO:0009507; C:chloroplast; HDA: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; IEA:InterPro.
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 2: Evidence at transcript level;
KW 4Fe-4S; Alternative splicing; 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..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..458
FT /note="5'-adenylylsulfate reductase 3, chloroplastic"
FT /id="PRO_0000023216"
FT DOMAIN 337..458
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..319
FT /note="Reductase domain"
FT ACT_SITE 378
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 381
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 378..381
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 28
FT /note="T -> A (in Ref. 2; AAC26978)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="D -> Y (in Ref. 2; AAC26978)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="N -> D (in Ref. 7; BAH57002)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="S -> T (in Ref. 8; AAM65133)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="A -> R (in Ref. 1; AAC49562)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="R -> I (in Ref. 1; AAC49562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 50695 MW; E950C28E15F418CB CRC64;
MALAINVSSS SSSAISSSSF PSSDLKVTKI GSLRLLNRTN VSAASLSLSG KRSSVKALNV
QSITKESIVA SEVTEKLDVV EVEDFEELAK RLENASPLEI MDKALEKFGN DIAIAFSGAE
DVALIEYAHL TGRPYRVFSL DTGRLNPETY RLFDTVEKHY GIRIEYMFPD AVEVQALVRN
KGLFSFYEDG HQECCRIRKV RPLRRALKGL RAWITGQRKD QSPGTRSEIP VVQVDPVFEG
LDGGVGSLVK WNPVANVEGN DVWNFLRTMD VPVNTLHAAG YVSIGCEPCT RAVLPGQHER
EGRWWWEDAK AKECGLHKGN IKENTNGNAT ANVNGTASVA DIFNSENVVN LSRQGIENLM
KLENRKEAWI VVLYAPWCPF CQAMEASFDE LADKLGGSGV KVAKFRADGD QKDFAKKELQ
LGSFPTILVF PKNSSRPIKY PSEKRDVDSL TSFLNLVR
