APK1_ARATH
ID APK1_ARATH Reviewed; 276 AA.
AC Q43295; Q8LES2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Adenylyl-sulfate kinase 1, chloroplastic;
DE EC=2.7.1.25 {ECO:0000305|PubMed:11488606};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 1;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase 1 {ECO:0000303|PubMed:19304933};
DE Short=APS kinase 1 {ECO:0000303|PubMed:11488606};
DE Flags: Precursor;
GN Name=APK1; Synonyms=AKN1 {ECO:0000303|PubMed:11488606};
GN OrderedLocusNames=At2g14750; ORFNames=F26C24.11, T6B13.1;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8049272; DOI=10.1016/0167-4781(94)90203-8;
RA Arz H.E., Gisselmann G., Schiffmann S., Schwenn J.-D.;
RT "A cDNA for adenylyl sulphate (APS)-kinase from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1218:447-452(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8066145; DOI=10.1104/pp.105.2.771;
RA Jain A., Leustek T.;
RT "A cDNA clone for 5'-adenylylphosphosulfate kinase from Arabidopsis
RT thaliana.";
RL Plant Physiol. 105:771-772(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9636674; DOI=10.1006/bbrc.1998.8751;
RA Lee S., Leustek T.;
RT "APS kinase from Arabidopsis thaliana: genomic organization, expression,
RT and kinetic analysis of the recombinant enzyme.";
RL Biochem. Biophys. Res. Commun. 247:171-175(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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 [7]
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 [8]
RP FUNCTION.
RX PubMed=7988678; DOI=10.1016/0014-5793(94)01193-1;
RA Schiffmann S., Schwenn J.D.;
RT "APS-sulfotransferase activity is identical to higher plant APS-kinase (EC
RT 2.7.1.25).";
RL FEBS Lett. 355:229-232(1994).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION
RP WITH AKN2, AND MUTAGENESIS OF SER-182.
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 [10]
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 [11]
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 [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 77-276 IN COMPLEX WITH SUBSTRATE,
RP AND MUTAGENESIS OF ASP-136.
RX PubMed=22810229; DOI=10.1074/jbc.m112.387001;
RA Ravilious G.E., Jez J.M.;
RT "Nucleotide binding site communication in Arabidopsis thaliana adenosine
RT 5'-phosphosulfate kinase.";
RL J. Biol. Chem. 287:30385-30394(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 77-276 IN COMPLEX WITH SUBSTRATE
RP AND ATP, SUBUNIT, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-86 AND CYS-119.
RX PubMed=22184237; DOI=10.1073/pnas.1115772108;
RA Ravilious G.E., Nguyen A., Francois J.A., Jez J.M.;
RT "Structural basis and evolution of redox regulation in plant adenosine-5'-
RT phosphosulfate kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:309-314(2012).
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, ECO:0000269|PubMed:7988678}.
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:0000305|PubMed:11488606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24153;
CC Evidence={ECO:0000305|PubMed:11488606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 uM for adenosine 5'-phosphosulfate
CC {ECO:0000269|PubMed:11488606};
CC KM=5.3 uM for adenosine 5'-phosphosulfate
CC {ECO:0000269|PubMed:19304933};
CC KM=147 uM for ATP {ECO:0000269|PubMed:11488606};
CC Vmax=7.35 mmol/min/mg enzyme {ECO:0000269|PubMed:11488606};
CC Vmax=20.1 mmol/min/mg enzyme {ECO:0000269|PubMed:19304933};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with APK2.
CC {ECO:0000269|PubMed:11488606, ECO:0000269|PubMed:22184237,
CC ECO:0000269|PubMed:22810229}.
CC -!- INTERACTION:
CC Q43295; Q43295: APK1; NbExp=3; IntAct=EBI-4438040, EBI-4438040;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19304933}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, root tips, leaf
CC epidermal and guard cells, pollen grains and funiculus of developing
CC seeds. {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; X75782; CAA53426.1; -; mRNA.
DR EMBL; U05238; AAC50035.1; -; mRNA.
DR EMBL; U59759; AAC50034.1; -; Genomic_DNA.
DR EMBL; AC004705; AAC24182.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06330.1; -; Genomic_DNA.
DR EMBL; AY054287; AAL06946.1; -; mRNA.
DR EMBL; AY132010; AAM91043.1; -; mRNA.
DR EMBL; AY085264; AAM62496.1; -; mRNA.
DR PIR; S47640; S47640.
DR RefSeq; NP_179082.1; NM_127039.4.
DR PDB; 3UIE; X-ray; 1.79 A; A/B/C=77-276.
DR PDB; 4FXP; X-ray; 1.95 A; A/B/C=77-276.
DR PDBsum; 3UIE; -.
DR PDBsum; 4FXP; -.
DR AlphaFoldDB; Q43295; -.
DR SMR; Q43295; -.
DR DIP; DIP-60003N; -.
DR IntAct; Q43295; 2.
DR STRING; 3702.AT2G14750.1; -.
DR iPTMnet; Q43295; -.
DR PaxDb; Q43295; -.
DR PRIDE; Q43295; -.
DR ProteomicsDB; 240608; -.
DR EnsemblPlants; AT2G14750.1; AT2G14750.1; AT2G14750.
DR GeneID; 815963; -.
DR Gramene; AT2G14750.1; AT2G14750.1; AT2G14750.
DR KEGG; ath:AT2G14750; -.
DR Araport; AT2G14750; -.
DR TAIR; locus:2046901; AT2G14750.
DR eggNOG; KOG0635; Eukaryota.
DR HOGENOM; CLU_046932_0_2_1; -.
DR OMA; MATEGHD; -.
DR OrthoDB; 1320063at2759; -.
DR PhylomeDB; Q43295; -.
DR BioCyc; ARA:AT2G14750-MON; -.
DR BioCyc; MetaCyc:AT2G14750-MON; -.
DR BRENDA; 2.7.1.25; 399.
DR SABIO-RK; Q43295; -.
DR UniPathway; UPA00140; UER00205.
DR PRO; PR:Q43295; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q43295; baseline and differential.
DR Genevisible; Q43295; 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; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA:TAIR.
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 3D-structure; Amino-acid biosynthesis; ATP-binding; Chloroplast;
KW Cysteine biosynthesis; Disulfide bond; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..276
FT /note="Adenylyl-sulfate kinase 1, chloroplastic"
FT /id="PRO_0000006635"
FT REGION 46..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 108..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22184237"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22184237,
FT ECO:0000269|PubMed:22810229"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22184237,
FT ECO:0000269|PubMed:22810229"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22184237,
FT ECO:0000269|PubMed:22810229"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22184237,
FT ECO:0000269|PubMed:22810229"
FT BINDING 181..182
FT /ligand="substrate"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22184237,
FT ECO:0000269|PubMed:22810229"
FT SITE 150
FT /note="Participates in a stacking interaction with the
FT adenine ring of adenylyl-sulfate"
FT DISULFID 86
FT /note="Interchain (with C-119)"
FT /evidence="ECO:0000269|PubMed:22184237"
FT DISULFID 119
FT /note="Interchain (with C-86)"
FT /evidence="ECO:0000269|PubMed:22184237"
FT MUTAGEN 86
FT /note="C->A: Increased catalytic efficiency in oxidative
FT conditions; when associated with Ala-119."
FT /evidence="ECO:0000269|PubMed:22184237"
FT MUTAGEN 119
FT /note="C->A: Increased catalytic efficiency in oxidative
FT conditions; when associated with Ala-86."
FT /evidence="ECO:0000269|PubMed:22184237"
FT MUTAGEN 136
FT /note="D->A,N: Decreases affinity for substrate and
FT catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:22810229"
FT MUTAGEN 182
FT /note="S->C,F: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:11488606"
FT CONFLICT 41
FT /note="M -> I (in Ref. 7; AAM62496)"
FT /evidence="ECO:0000305"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:3UIE"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3UIE"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3UIE"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3UIE"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3UIE"
FT TURN 141..147
FT /evidence="ECO:0007829|PDB:3UIE"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:3UIE"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3UIE"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:3UIE"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:3UIE"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:3UIE"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3UIE"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3UIE"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3UIE"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:3UIE"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3UIE"
SQ SEQUENCE 276 AA; 29787 MW; CB698643AA09D811 CRC64;
MIAAGAKSLL GLSMASPKGI FDSNSMSNSR SVVVVRACVS MDGSQTLSHN KNGSIPEVKS
INGHTGQKQG PLSTVGNSTN IKWHECSVEK VDRQRLLDQK GCVIWVTGLS GSGKSTLACA
LNQMLYQKGK LCYILDGDNV RHGLNRDLSF KAEDRAENIR RVGEVAKLFA DAGIICIASL
ISPYRTDRDA CRSLLPEGDF VEVFMDVPLS VCEARDPKGL YKLARAGKIK GFTGIDDPYE
PPLNCEISLG REGGTSPIEM AEKVVGYLDN KGYLQA
