APK2_ARATH
ID APK2_ARATH Reviewed; 293 AA.
AC O49196;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Adenylyl-sulfate kinase 2, chloroplastic;
DE EC=2.7.1.25;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 2;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase 2;
DE Short=APS kinase 2;
DE Flags: Precursor;
GN Name=APK2; Synonyms=AKN2; OrderedLocusNames=At4g39940; ORFNames=T5J17.110;
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].
RC STRAIN=cv. Columbia;
RA Schiffmann S., Schwenn J.-D.;
RT "Isolation of cDNA clones encoding adenosine-5'-phosphosulfate-kinase (EC
RT 2.7.1.25) from Catharanthus roseus and an isoform (akn2) from
RT Arabidopsis.";
RL (er) Plant Gene Register PGR98-116(1998).
RN [2]
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 [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 FUNCTION, AND INTERACTION WITH AKN1.
RX PubMed=11488606; DOI=10.1006/abbi.2001.2453;
RA Lillig C.H., Schiffmann S., Berndt C., Berken A., Tischka R., Schwenn J.D.;
RT "Molecular and catalytic properties of Arabidopsis thaliana adenylyl
RT sulfate (APS)-kinase.";
RL Arch. Biochem. Biophys. 392:303-310(2001).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP 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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [8]
RP FUNCTION.
RX PubMed=23218016; DOI=10.1016/j.phytochem.2012.11.006;
RA Badenes-Perez F.R., Reichelt M., Gershenzon J., Heckel D.G.;
RT "Interaction of glucosinolate content of Arabidopsis thaliana mutant lines
RT and feeding and oviposition by generalist and specialist lepidopterans.";
RL Phytochemistry 86:36-43(2013).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate. Essential for
CC plant reproduction and viability. Required for the production of
CC glucosinolates. {ECO:0000269|PubMed:11488606,
CC ECO:0000269|PubMed:19304933, ECO:0000269|PubMed:19903478,
CC ECO:0000269|PubMed:23218016}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for adenylyl sulfate {ECO:0000269|PubMed:19304933};
CC Vmax=10.6 mmol/min/mg enzyme {ECO:0000269|PubMed:19304933};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SUBUNIT: Interacts with APK1. {ECO:0000269|PubMed:11488606}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19304933}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, root tips, leaf
CC epidermal cells and funiculus of developing seeds.
CC {ECO:0000269|PubMed:19304933}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Apk1 and apk2 double mutant exhibits a semi-dwarf
CC phenotype. {ECO:0000269|PubMed:19304933, ECO:0000269|PubMed:19903478}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; AF043351; AAC39520.1; -; mRNA.
DR EMBL; AL035708; CAB38907.1; -; Genomic_DNA.
DR EMBL; AL161596; CAB80657.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87142.1; -; Genomic_DNA.
DR EMBL; AF462823; AAL58913.1; -; mRNA.
DR EMBL; AY097421; AAM19937.1; -; mRNA.
DR PIR; T06100; T06100.
DR RefSeq; NP_195704.1; NM_120157.4.
DR AlphaFoldDB; O49196; -.
DR SMR; O49196; -.
DR BioGRID; 15433; 1.
DR IntAct; O49196; 3.
DR STRING; 3702.AT4G39940.1; -.
DR PaxDb; O49196; -.
DR PRIDE; O49196; -.
DR ProteomicsDB; 246950; -.
DR EnsemblPlants; AT4G39940.1; AT4G39940.1; AT4G39940.
DR GeneID; 830153; -.
DR Gramene; AT4G39940.1; AT4G39940.1; AT4G39940.
DR KEGG; ath:AT4G39940; -.
DR Araport; AT4G39940; -.
DR TAIR; locus:2140005; AT4G39940.
DR eggNOG; KOG0635; Eukaryota.
DR HOGENOM; CLU_046932_0_2_1; -.
DR InParanoid; O49196; -.
DR OMA; NIRWHDC; -.
DR OrthoDB; 1320063at2759; -.
DR PhylomeDB; O49196; -.
DR BioCyc; ARA:AT4G39940-MON; -.
DR BioCyc; MetaCyc:AT4G39940-MON; -.
DR BRENDA; 2.7.1.25; 399.
DR SABIO-RK; O49196; -.
DR UniPathway; UPA00140; UER00205.
DR PRO; PR:O49196; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49196; baseline and differential.
DR Genevisible; O49196; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009536; C:plastid; TAS: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: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; Chloroplast; Cysteine biosynthesis;
KW Kinase; Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..293
FT /note="Adenylyl-sulfate kinase 2, chloroplastic"
FT /id="PRO_0000006636"
FT ACT_SITE 196
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 122..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195..196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Participates in a stacking interaction with the
FT adenine ring of adenylyl-sulfate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 31977 MW; 71F1AD6E9B026886 CRC64;
MEGLAIRASR PSVFCSIPGL GGDSHRKPPS DGFLKLPASS IPADSRKLVA NSTSFHPISA
VNVSAQASLT ADFPALSETI LKEGRNNGKE KAENIVWHES SICRCDRQQL LQQKGCVVWI
TGLSGSGKST VACALSKALF ERGKLTYTLD GDNVRHGLNR DLTFKAEHRT ENIRRIGEVA
KLFADVGVIC IASLISPYRR DRDACRSLLP DGDFVEVFMD VPLHVCESRD PKGLYKLARA
GKIKGFTGID DPYEAPVNCE VVLKHTGDDE SCSPRQMAEN IISYLQNKGY LEG
