APS1_ARATH
ID APS1_ARATH Reviewed; 463 AA.
AC Q9LIK9; Q42278; Q42519; Q56Z36; Q8LDJ6; Q9SE02;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ATP sulfurylase 1, chloroplastic;
DE Short=AtPS1;
DE EC=2.7.7.4;
DE Flags: Precursor;
GN Name=APS1; OrderedLocusNames=At3g22890; ORFNames=F5N5.6;
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], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8058839; DOI=10.1104/pp.105.3.897;
RA Leustek T., Murillo M., Cervantes M.;
RT "Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by
RT functional expression in Saccharomyces cerevisiae.";
RL Plant Physiol. 105:897-902(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10806350; DOI=10.1016/s0378-1119(00)00132-3;
RA Hatzfeld Y., Lee S., Lee M., Leustek T., Saito K.;
RT "Functional characterization of a gene encoding a fourth ATP sulfurylase
RT isoform from Arabidopsis thaliana.";
RL Gene 248:51-58(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 1-93.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Desprez T., Amselem J., Chiapello H., Caboche M., Hofte H.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INDUCTION BY GSH.
RX PubMed=10341446; DOI=10.1046/j.1365-313x.1999.00416.x;
RA Lappartient A.G., Vidmar J.J., Leustek T., Glass A.D.M., Touraine B.;
RT "Inter-organ signaling in plants: regulation of ATP sulfurylase and sulfate
RT transporter genes expression in roots mediated by phloem-translocated
RT compound.";
RL Plant J. 18:89-95(1999).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9880353; DOI=10.1104/pp.119.1.123;
RA Pilon-Smits E.A.H., Hwang S., Mel Lytle C., Zhu Y., Tai J.C., Bravo R.C.,
RA Chen Y., Leustek T., Terry N.;
RT "Overexpression of ATP sulfurylase in indian mustard leads to increased
RT selenate uptake, reduction, and tolerance.";
RL Plant Physiol. 119:123-132(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: Mediates selenate (Se) reduction, and promotes Se and sulfur
CC (S) uptake and assimilation. {ECO:0000269|PubMed:9880353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:8058839,
CC ECO:0000269|PubMed:9880353};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:8058839}.
CC -!- INDUCTION: Repressed locally and systemically by phloem-translocated
CC glutathione (GSH). {ECO:0000269|PubMed:10341446}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA21570.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF19185.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD95100.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U05218; AAA21570.1; ALT_FRAME; mRNA.
DR EMBL; AF198964; AAF19185.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AP001300; BAB03034.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76688.1; -; Genomic_DNA.
DR EMBL; AF370492; AAK43869.1; -; mRNA.
DR EMBL; AY050869; AAK92806.1; -; mRNA.
DR EMBL; AY054169; AAL06830.1; -; mRNA.
DR EMBL; AY064648; AAL47359.1; -; mRNA.
DR EMBL; AY091207; AAM14146.1; -; mRNA.
DR EMBL; BT002538; AAO00898.1; -; mRNA.
DR EMBL; AK221133; BAD95100.1; ALT_INIT; mRNA.
DR EMBL; AK226559; BAE98690.1; -; mRNA.
DR EMBL; AY085975; AAM63185.1; -; mRNA.
DR EMBL; Z34534; CAA84304.1; -; mRNA.
DR RefSeq; NP_188929.1; NM_113189.5.
DR AlphaFoldDB; Q9LIK9; -.
DR SMR; Q9LIK9; -.
DR BioGRID; 7193; 3.
DR STRING; 3702.AT3G22890.1; -.
DR MetOSite; Q9LIK9; -.
DR PaxDb; Q9LIK9; -.
DR PRIDE; Q9LIK9; -.
DR ProteomicsDB; 244477; -.
DR EnsemblPlants; AT3G22890.1; AT3G22890.1; AT3G22890.
DR GeneID; 821861; -.
DR Gramene; AT3G22890.1; AT3G22890.1; AT3G22890.
DR KEGG; ath:AT3G22890; -.
DR Araport; AT3G22890; -.
DR TAIR; locus:2084563; AT3G22890.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_009463_2_0_1; -.
DR OMA; DQMYERP; -.
DR OrthoDB; 528280at2759; -.
DR PhylomeDB; Q9LIK9; -.
DR BioCyc; ARA:AT3G22890-MON; -.
DR BioCyc; MetaCyc:AT3G22890-MON; -.
DR BRENDA; 2.7.7.4; 399.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:Q9LIK9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIK9; baseline and differential.
DR Genevisible; Q9LIK9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; TAS:TAIR.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0001887; P:selenium compound metabolic process; IMP:TAIR.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Nucleotide-binding; Nucleotidyltransferase;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 49..463
FT /note="ATP sulfurylase 1, chloroplastic"
FT /id="PRO_0000410869"
FT CONFLICT 60
FT /note="E -> G (in Ref. 1; AAA21570)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="A -> T (in Ref. 7; AAM63185)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> S (in Ref. 7; AAM63185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 51459 MW; F05DFD8F86CF25C8 CRC64;
MASMAAVLSK TPFLSQPLTK SSPNSDLPFA AVSFPSKSLR RRVGSIRAGL IAPDGGKLVE
LIVEEPKRRE KKHEAADLPR VELTAIDLQW MHVLSEGWAS PLGGFMRESE FLQTLHFNSL
RLDDGSVVNM SVPIVLAIDD EQKARIGEST RVALFNSDGN PVAILSDIEI YKHPKEERIA
RTWGTTAPGL PYVDEAITNA GNWLIGGDLE VLEPVKYNDG LDRFRLSPAE LRKELEKRNA
DAVFAFQLRN PVHNGHALLM TDTRRRLLEM GYKNPILLLH PLGGFTKADD VPLDWRMKQH
EKVLEDGVLD PETTVVSIFP SPMHYAGPTE VQWHAKARIN AGANFYIVGR DPAGMGHPVE
KRDLYDADHG KKVLSMAPGL ERLNILPFRV AAYDKTQGKM AFFDPSRPQD FLFISGTKMR
TLAKNNENPP DGFMCPGGWK VLVDYYESLT PAGNGRLPEV VPV
