APK3_ARATH
ID APK3_ARATH Reviewed; 208 AA.
AC Q9SRW7; Q9SQR9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Adenylyl-sulfate kinase 3 {ECO:0000305};
DE EC=2.7.1.25 {ECO:0000269|PubMed:19304933};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 3;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase 3 {ECO:0000303|PubMed:19304933};
DE Short=APS kinase 3 {ECO:0000303|PubMed:19304933};
GN Name=APK3 {ECO:0000303|PubMed:19304933}; OrderedLocusNames=At3g03900;
GN ORFNames=F20H23.5, T11I18.1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19304933; DOI=10.1105/tpc.109.065581;
RA Mugford S.G., Yoshimoto N., Reichelt M., Wirtz M., Hill L., Mugford S.T.,
RA Nakazato Y., Noji M., Takahashi H., Kramell R., Gigolashvili T.,
RA Fluegge U.I., Wasternack C., Gershenzon J., Hell R., Saito K., Kopriva S.;
RT "Disruption of adenosine-5'-phosphosulfate kinase in Arabidopsis reduces
RT levels of sulfated secondary metabolites.";
RL Plant Cell 21:910-927(2009).
RN [4]
RP FUNCTION.
RX PubMed=19903478; DOI=10.1016/j.febslet.2009.11.014;
RA Mugford S.G., Matthewman C.A., Hill L., Kopriva S.;
RT "Adenosine-5'-phosphosulfate kinase is essential for Arabidopsis
RT viability.";
RL FEBS Lett. 584:119-123(2010).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate for the
CC sulfation of secondary metabolites, including the glucosinolates
CC (PubMed:19304933). Essential for plant reproduction and viability
CC (PubMed:19903478). {ECO:0000269|PubMed:19304933,
CC ECO:0000269|PubMed:19903478}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000269|PubMed:19304933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24153;
CC Evidence={ECO:0000269|PubMed:19304933};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 uM for adenylyl sulfate {ECO:0000269|PubMed:19304933};
CC Vmax=12.4 mmol/min/mg enzyme {ECO:0000269|PubMed:19304933};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19304933}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, root tips, leaf
CC epidermal and guard cells, pollen grains and radicle of immature seeds.
CC {ECO:0000269|PubMed:19304933}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19304933}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC009540; AAF00628.1; -; Genomic_DNA.
DR EMBL; AC011698; AAF05850.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74010.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65534.1; -; Genomic_DNA.
DR RefSeq; NP_001319463.1; NM_001337491.1.
DR RefSeq; NP_001327493.1; NM_001337492.1.
DR AlphaFoldDB; Q9SRW7; -.
DR SMR; Q9SRW7; -.
DR STRING; 3702.AT3G03900.1; -.
DR PaxDb; Q9SRW7; -.
DR PRIDE; Q9SRW7; -.
DR ProteomicsDB; 246951; -.
DR EnsemblPlants; AT3G03900.1; AT3G03900.1; AT3G03900.
DR EnsemblPlants; AT3G03900.2; AT3G03900.2; AT3G03900.
DR GeneID; 821077; -.
DR Gramene; AT3G03900.1; AT3G03900.1; AT3G03900.
DR Gramene; AT3G03900.2; AT3G03900.2; AT3G03900.
DR KEGG; ath:AT3G03900; -.
DR Araport; AT3G03900; -.
DR TAIR; locus:2079379; AT3G03900.
DR eggNOG; KOG0635; Eukaryota.
DR HOGENOM; CLU_046932_1_0_1; -.
DR InParanoid; Q9SRW7; -.
DR OMA; GVTIWFT; -.
DR OrthoDB; 1320063at2759; -.
DR PhylomeDB; Q9SRW7; -.
DR BioCyc; ARA:AT3G03900-MON; -.
DR SABIO-RK; Q9SRW7; -.
DR UniPathway; UPA00140; UER00205.
DR PRO; PR:Q9SRW7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRW7; baseline and differential.
DR Genevisible; Q9SRW7; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis; Cytoplasm;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="Adenylyl-sulfate kinase 3"
FT /id="PRO_0000424066"
FT ACT_SITE 111
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
FT SITE 79
FT /note="Participates in a stacking interaction with the
FT adenine ring of adenylyl-sulfate"
FT /evidence="ECO:0000250|UniProtKB:Q43295"
SQ SEQUENCE 208 AA; 23146 MW; 2BA510DC0F35EA33 CRC64;
MSTVGNSTNI FWQESPIGKT ERQKLLNQKG CVVWITGLSG SGKSTLACSL SRELNNRGKL
SYILDGDNLR HGLNKDLGFK AEDRVENIRR VGEVAKLFAD AGLICIASLI SPYRKDRDAC
REMIQNSSFI EVFMNMSLQL CEARDPKGLY KLARAGKIKG FTGIDDPYES PLNCEIELKE
KEGECPSPVA MAEEVISYLE DKGFLQNE
