APS3_ARATH
ID APS3_ARATH Reviewed; 465 AA.
AC O23324; Q42520; Q96530;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ATP-sulfurylase 3, chloroplastic;
DE EC=2.7.7.4;
DE Flags: Precursor;
GN Name=APS3; OrderedLocusNames=At4g14680; ORFNames=dl3380c, FCAALL.128;
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], HOMOTETRAMERIZATION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7487067; DOI=10.1006/abbi.1995.0026;
RA Murillo M., Leustek T.;
RT "Adenosine-5'-triphosphate-sulfurylase from Arabidopsis thaliana and
RT Escherichia coli are functionally equivalent but structurally and
RT kinetically divergent: nucleotide sequence of two adenosine-5'-
RT triphosphate-sulfurylase cDNAs from Arabidopsis thaliana and analysis of a
RT recombinant enzyme.";
RL Arch. Biochem. Biophys. 323:195-204(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(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 INDUCTION BY S STARVATION.
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).
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:7487067};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC -!- INDUCTION: Accumulates in roots during S starvation, but decreased
CC after SO(4) anion restoration (at protein level). Repressed locally and
CC systemically by phloem-translocated glutathione (GSH) (at protein
CC level). {ECO:0000269|PubMed:10341446}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U06275; AAA92350.1; -; mRNA.
DR EMBL; U59738; AAB09473.1; -; Genomic_DNA.
DR EMBL; Z97336; CAB10247.1; -; Genomic_DNA.
DR EMBL; AL161539; CAB78510.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83474.1; -; Genomic_DNA.
DR PIR; E71409; E71409.
DR RefSeq; NP_193204.1; NM_117550.5.
DR AlphaFoldDB; O23324; -.
DR SMR; O23324; -.
DR BioGRID; 12415; 1.
DR STRING; 3702.AT4G14680.1; -.
DR PaxDb; O23324; -.
DR PRIDE; O23324; -.
DR ProteomicsDB; 246913; -.
DR EnsemblPlants; AT4G14680.1; AT4G14680.1; AT4G14680.
DR GeneID; 827118; -.
DR Gramene; AT4G14680.1; AT4G14680.1; AT4G14680.
DR KEGG; ath:AT4G14680; -.
DR Araport; AT4G14680; -.
DR TAIR; locus:2130080; AT4G14680.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_009463_2_0_1; -.
DR InParanoid; O23324; -.
DR OMA; ESQCKKV; -.
DR PhylomeDB; O23324; -.
DR BioCyc; MetaCyc:AT4G14680-MON; -.
DR BRENDA; 2.7.7.4; 399.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:O23324; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23324; baseline and differential.
DR Genevisible; O23324; AT.
DR GO; GO:0009507; C:chloroplast; NAS:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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; IMP:TAIR.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IEP:UniProtKB.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0070206; P:protein trimerization; IDA:UniProtKB.
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..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..465
FT /note="ATP-sulfurylase 3, chloroplastic"
FT /id="PRO_0000410870"
FT CONFLICT 7
FT /note="V -> D (in Ref. 1; AAA92350)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="S -> A (in Ref. 1; AAA92350/AAB09473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 52030 MW; 1D79E72B28FE4CCB CRC64;
MASMSTVFPK PTSFISQPLT KSHKSDSVTT SISFPSNSKT RSLRTISVRA GLIEPDGGKL
VDLVVPEPRR REKKHEAADL PRVRLTAIDL QWMHVLSEGW ASPLRGFMRE SEFLQTLHFN
LLNLDDGSVV NMSVPIVLAI DDQQKALIGE SKRVSLVDSD DNPIAILNDI EIYKHPKEER
IARTWGTTAP GLPYVEEAIT NAGDWLIGGD LEVLEPVKYN DGLDRFRLSP FELRKELEKR
GADAVFAFQL RNPVHNGHAL LMTDTRRRLL EMGYKNPILL LHPLGGFTKA DDVPLSWRMK
QHEKVLEDGV LDPETTVVSI FPSPMLYAGP TEVQWHAKAR INAGANFYIV GRDPAGMGHP
VEKRDLYDAD HGKKVLSMAP GLERLNILPF RVAAYDKTQG KMAFFDPSRA QDFLFISGTK
MRALAKNREN PPDGFMCPGG WKVLVDYYDS LTLTGNTKLP EKIPV
