APS4_ARATH
ID APS4_ARATH Reviewed; 469 AA.
AC Q9S7D8; Q0WWX9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ATP sulfurylase 4, chloroplastic;
DE EC=2.7.7.4 {ECO:0000269|PubMed:10806350};
DE Flags: Precursor;
GN Name=APS4; OrderedLocusNames=At5g43780; ORFNames=MQD19.13;
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, AND TRANSIT PEPTIDE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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.
CC -!- FUNCTION: Sulfate adenylyltransferase. Catalyzes the first step of the
CC sulfate assimilation pathway. {ECO:0000269|PubMed:10806350}.
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;
CC Evidence={ECO:0000269|PubMed:10806350};
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:10806350}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:10806350}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF110407; AAD26634.1; -; Genomic_DNA.
DR EMBL; AJ012586; CAB42640.1; -; mRNA.
DR EMBL; AB026651; BAB11306.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95009.1; -; Genomic_DNA.
DR EMBL; AY072193; AAL60015.1; -; mRNA.
DR EMBL; AY117323; AAM51398.1; -; mRNA.
DR EMBL; AK226204; BAE98369.1; -; mRNA.
DR PIR; T52659; T52659.
DR RefSeq; NP_199191.1; NM_123745.6.
DR AlphaFoldDB; Q9S7D8; -.
DR SMR; Q9S7D8; -.
DR BioGRID; 19650; 1.
DR STRING; 3702.AT5G43780.1; -.
DR PaxDb; Q9S7D8; -.
DR PRIDE; Q9S7D8; -.
DR ProteomicsDB; 244463; -.
DR EnsemblPlants; AT5G43780.1; AT5G43780.1; AT5G43780.
DR GeneID; 834400; -.
DR Gramene; AT5G43780.1; AT5G43780.1; AT5G43780.
DR KEGG; ath:AT5G43780; -.
DR Araport; AT5G43780; -.
DR TAIR; locus:2170867; AT5G43780.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_009463_2_0_1; -.
DR InParanoid; Q9S7D8; -.
DR OMA; IDVQWMH; -.
DR OrthoDB; 528280at2759; -.
DR PhylomeDB; Q9S7D8; -.
DR BioCyc; MetaCyc:AT5G43780-MON; -.
DR BRENDA; 2.7.7.4; 399.
DR UniPathway; UPA00140; UER00204.
DR PRO; PR:Q9S7D8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7D8; baseline and differential.
DR Genevisible; Q9S7D8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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: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 ATP-binding; Chloroplast; Nucleotide-binding; Nucleotidyltransferase;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:10806350"
FT CHAIN 52..469
FT /note="ATP sulfurylase 4, chloroplastic"
FT /id="PRO_0000410871"
FT CONFLICT 171
FT /note="D -> E (in Ref. 5; BAE98369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 52126 MW; A4665C48E57562ED CRC64;
MASSAAAIVS GSPFRSSPLI HNHHASRYAP GSISVVSLPR QVSRRGLSVK SGLIEPDGGK
LMNLVVEESR RRVMKHEAET VPARIKLNRV DLEWVHVLSE GWASPLKGFM RQSEFLQTLH
FNSFRLEDGS VVNMSVPIVL AIDDDQKFRI GDSNQVTLVD SVGNPIAILN DIEIYKHPKE
ERIARTWGTT ARGLPYAEEA ITKAGNWLIG GDLQVLEPIK YNDGLDRFRL SPSQLREEFI
RRGADAVFAF QLRNPVHNGH ALLMTDTRRR LLEMGYKNPV LLLNPLGGFT KADDVPLSWR
MRQHEKVLED GVLDPETTVV SIFPSPMLYA GPTEVQWHAK ARINAGANFY IVGRDPAGMG
HPTEKRDLYD ADHGKKVLSM APGLERLNIL PFKVAAYDKT QGKMAFFDPS RSQDFLFISG
TKMRGLAKKK ENPPDGFMCP SGWKVLVDYY DSLSAETGNG RVSEAVASA
