APR2_ARATH
ID APR2_ARATH Reviewed; 454 AA.
AC P92981; O04215; O04583; O22554; Q38947; Q541D4;
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 2, chloroplastic;
DE EC=1.8.4.9;
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate reductase homolog 43;
DE Short=PAPS reductase homolog 43;
DE Short=Prh-43;
DE AltName: Full=Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 2;
DE Short=APS sulfotransferase 2;
DE AltName: Full=Thioredoxin-independent APS reductase 2;
DE Flags: Precursor;
GN Name=APR2; Synonyms=APSR, PRH43; OrderedLocusNames=At1g62180;
GN ORFNames=F19K23.11;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Min B., Shin K.W., Ye X., Lee S.Y.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Gutierrez-Marcos J.F., Campbell E.I., Wray J.L.;
RT "A fourth member of the APS reductase gene family in Arabidopsis
RT thaliana.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [6]
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 [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 [GENOMIC DNA / MRNA] OF 45-454.
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 [10]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF CYS-195 AND CYS-314.
RX PubMed=11553635; DOI=10.1074/jbc.m107424200;
RA Kopriva S., Buechert T., Fritz G., Suter M., Weber M., Benda R.,
RA Schaller J., Feller U., Schuermann P., Schuenemann V., Trautwein A.X.,
RA Kroneck P.M., Brunold C.;
RT "Plant adenosine 5'-phosphosulfate reductase is a novel iron-sulfur
RT protein.";
RL J. Biol. Chem. 276:42881-42886(2001).
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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-67, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ARG-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 {ECO:0000269|PubMed:11553635}.
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;
CC Evidence={ECO:0000269|PubMed:11553635};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:11553635};
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=P92981-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Leaves 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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APS reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC26977.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U53866; AAC49563.1; -; mRNA.
DR EMBL; AF023167; AAB80957.1; -; mRNA.
DR EMBL; U96045; AAB57688.1; -; mRNA.
DR EMBL; AF016283; AAC26980.1; -; Genomic_DNA.
DR EMBL; AC000375; AAB60764.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33931.1; -; Genomic_DNA.
DR EMBL; AF360192; AAK25902.1; -; mRNA.
DR EMBL; AY040005; AAK64082.1; -; mRNA.
DR EMBL; AY088665; AAM66987.1; -; mRNA.
DR EMBL; U56921; AAC26977.1; ALT_INIT; mRNA.
DR PIR; C96648; C96648.
DR RefSeq; NP_176409.1; NM_104899.3. [P92981-1]
DR AlphaFoldDB; P92981; -.
DR SMR; P92981; -.
DR BioGRID; 27735; 1.
DR IntAct; P92981; 1.
DR STRING; 3702.AT1G62180.1; -.
DR iPTMnet; P92981; -.
DR MetOSite; P92981; -.
DR PaxDb; P92981; -.
DR PRIDE; P92981; -.
DR ProteomicsDB; 244426; -. [P92981-1]
DR EnsemblPlants; AT1G62180.1; AT1G62180.1; AT1G62180. [P92981-1]
DR GeneID; 842514; -.
DR Gramene; AT1G62180.1; AT1G62180.1; AT1G62180. [P92981-1]
DR KEGG; ath:AT1G62180; -.
DR Araport; AT1G62180; -.
DR TAIR; locus:2018097; AT1G62180.
DR eggNOG; KOG0189; Eukaryota.
DR eggNOG; KOG0191; Eukaryota.
DR OMA; WDFLRVM; -.
DR OrthoDB; 834258at2759; -.
DR PhylomeDB; P92981; -.
DR BioCyc; MetaCyc:AT1G62180-MON; -.
DR BRENDA; 1.8.4.9; 399.
DR PRO; PR:P92981; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92981; baseline and differential.
DR Genevisible; P92981; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA: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; IDA:TAIR.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IDA:TAIR.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); TAS: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 Acetylation; Alternative splicing; Amino-acid biosynthesis; Chloroplast;
KW Cysteine biosynthesis; Disulfide bond; Oxidoreductase; Plastid;
KW Redox-active center; Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 67..454
FT /note="5'-adenylylsulfate reductase 2, chloroplastic"
FT /id="PRO_0000023215"
FT DOMAIN 333..454
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..319
FT /note="Reductase domain"
FT ACT_SITE 374
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 377
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 374..377
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 195
FT /note="C->S: Slightly reduces activity."
FT /evidence="ECO:0000269|PubMed:11553635"
FT MUTAGEN 314
FT /note="C->S: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:11553635"
FT CONFLICT 16
FT /note="S -> T (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="T -> N (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="S -> A (in Ref. 1; AAC49563)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..48
FT /note="YS -> P (in Ref. 1; AAC49563)"
FT /evidence="ECO:0000305"
FT CONFLICT 57..58
FT /note="HS -> SHT (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="T -> L (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="G -> E (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="R -> K (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="Q -> E (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="R -> S (in Ref. 9; AAC26977)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="K -> F (in Ref. 9; AAC26977)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="K -> R (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="G -> R (in Ref. 9; AAC26977)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="I -> V (in Ref. 3; AAB57688 and 8; AAM66987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 50656 MW; 4EB93C1FFC5E4636 CRC64;
MALAVTSSST AISGSSFSRS GASSESKALQ ICSIRLSDRT HLSQRRYSMK PLNAESHSRS
ESWVTRASTL IAPEVEEKGG EVEDFEQLAK KLEDASPLEI MDKALERFGD QIAIAFSGAE
DVALIEYARL TGKPFRVFSL DTGRLNPETY RLFDAVEKQY GIRIEYMFPD AVEVQALVRN
KGLFSFYEDG HQECCRVRKV RPLRRALKGL KAWITGQRKD QSPGTRSEIP IVQVDPVFEG
LDGGVGSLVK WNPLANVEGA DVWNFLRTMD VPVNALHAQG YVSIGCEPCT RPVLPGQHER
EGRWWWEDAK AKECGLHKGN IKEEDGAADS KPAAVQEIFE SNNVVALSKG GVENLLKLEN
RKEAWLVVLY APWCPFCQAM EASYIELAEK LAGKGVKVAK FRADGEQKEF AKQELQLGSF
PTILLFPKRA PRAIKYPSEH RDVDSLMSFV NLLR
