APS2_ARATH
ID APS2_ARATH Reviewed; 476 AA.
AC Q43870; Q8LDB2; Q8RWJ3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP sulfurylase 2;
DE EC=2.7.7.4;
DE Flags: Precursor;
GN Name=APS2; Synonyms=ASA1, MET3-1; OrderedLocusNames=At1g19920;
GN ORFNames=F6F9.2;
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 PROBABLE ALTERNATIVE
RP INITIATION.
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 [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX PubMed=7724678; DOI=10.1104/pp.107.2.653;
RA Klonus D., Riesmeier J.W., Willmitzer L.;
RT "A cDNA clone for an ATP-sulfurylase from Arabidopsis thaliana.";
RL Plant Physiol. 107:653-654(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP INDUCTION BY SULFUR STARVATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8647819; DOI=10.1074/jbc.271.21.12227;
RA Logan H.M., Cathala N., Grignon C., Davidian J.-C.;
RT "Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP
RT sulfurylase multigene family. Expression studies in yeast and in relation
RT to plant sulfur nutrition.";
RL J. Biol. Chem. 271:12227-12233(1996).
RN [4]
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 [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 CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9536047; DOI=10.1104/pp.116.4.1307;
RA Hatzfeld Y., Cathala N., Grignon C., Davidian J.-C.;
RT "Effect of ATP sulfurylase overexpression in bright yellow 2 tobacco cells.
RT Regulation Of atp sulfurylase and SO4(2-) transport activities.";
RL Plant Physiol. 116:1307-1313(1998).
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 ECO:0000269|PubMed:8647819, ECO:0000269|PubMed:9536047};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q43870-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q43870-2; Sequence=VSP_041553;
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves or cotyledons.
CC {ECO:0000269|PubMed:8647819}.
CC -!- INDUCTION: In roots, upon sulfur starvation.
CC {ECO:0000269|PubMed:8647819}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U06276; AAA92351.1; -; mRNA.
DR EMBL; X79210; CAA55799.1; -; mRNA.
DR EMBL; U40715; AAC49324.1; -; mRNA.
DR EMBL; U59737; AAB09471.1; -; Genomic_DNA.
DR EMBL; AC007797; AAG12541.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29913.1; -; Genomic_DNA.
DR EMBL; AY093049; AAM13048.1; -; mRNA.
DR EMBL; BT000417; AAN15736.1; -; mRNA.
DR EMBL; AY086101; AAM63309.1; -; mRNA.
DR PIR; S44943; S44943.
DR RefSeq; NP_564099.1; NM_101847.4. [Q43870-1]
DR AlphaFoldDB; Q43870; -.
DR SMR; Q43870; -.
DR BioGRID; 23819; 1.
DR IntAct; Q43870; 1.
DR STRING; 3702.AT1G19920.1; -.
DR MetOSite; Q43870; -.
DR PaxDb; Q43870; -.
DR PRIDE; Q43870; -.
DR ProteomicsDB; 244454; -. [Q43870-1]
DR EnsemblPlants; AT1G19920.1; AT1G19920.1; AT1G19920. [Q43870-1]
DR GeneID; 838580; -.
DR Gramene; AT1G19920.1; AT1G19920.1; AT1G19920. [Q43870-1]
DR KEGG; ath:AT1G19920; -.
DR Araport; AT1G19920; -.
DR TAIR; locus:2035395; AT1G19920.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_009463_2_0_1; -.
DR InParanoid; Q43870; -.
DR OMA; ANARKIH; -.
DR PhylomeDB; Q43870; -.
DR BioCyc; MetaCyc:AT1G19920-MON; -.
DR BRENDA; 2.7.7.4; 399.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:Q43870; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q43870; baseline and differential.
DR Genevisible; Q43870; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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; 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: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 Alternative initiation; ATP-binding; Chloroplast; Cytoplasm;
KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..476
FT /note="ATP sulfurylase 2"
FT /id="PRO_5000144796"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041553"
FT CONFLICT 453
FT /note="W -> R (in Ref. 7; AAM13048/AAN15736)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="S -> K (in Ref. 8; AAM63309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53638 MW; 119FF1A7C10DE9C8 CRC64;
MSLMIRSSYV SHITLFQPRN SKPSSFTNQI SFLSSSNNNP FLNLVYKRNL TMQSVSKMTV
KSSLIDPDGG ELVELIVPET EIGVKKAESE TMPKVKLNQI DLEWVHVISE GWASPLKGFM
REDEYLQSLH FNSLRLKNGT FVNMSLPIVL AIDDDTKEQI GSSENVALVC PQGDIIGSLR
SVEIYKHNKE ERIARTWGTT SPGLPYVEEY ITPSGNWLIG GDLEVFEPIK YNDGLDHYRL
SPKQLREEFD NRQADAVFAF QLRNPVHNGH ALLMNDTRKR LLEMGYKNPV LLLHPLGGFT
KADDVPLDVR MEQHSKVLED GVLDPKTTIV SIFPSPMHYA GPTEVQWHAK ARINAGANFY
IVGRDPAGMG HPTEKRDLYD PDHGKRVLSM APGLEKLNIL PFRVAAYDTI EKKMAFFDPS
RAKEFLFISG TKMRTYARTG ENPPDGFMCP SGWNVLVKYY ESLQESEAKQ QAVVSA
