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Protein

Adenylyl-sulfate kinase 1, chloroplastic

Gene

APK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates.5 Publications

Catalytic activityi

ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.

Kineticsi

  1. KM=0.14 µM for adenylyl sulfate2 Publications
  2. KM=5.1 µM for adenylyl sulfate2 Publications
  3. KM=147 µM for ATP2 Publications
  1. Vmax=7.35 mmol/min/mg enzyme2 Publications
  2. Vmax=20.1 mmol/min/mg enzyme2 Publications

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes sulfite from sulfate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. ATP sulfurylase 4, chloroplastic (APS4), ATP-sulfurylase 3, chloroplastic (APS3), ATP sulfurylase 2 (APS2), ATP sulfurylase 1, chloroplastic (APS1)
  2. Adenylyl-sulfate kinase 4, chloroplastic (APK4), Adenylyl-sulfate kinase 1, chloroplastic (APK1), Adenylyl-sulfate kinase 3 (APK3), Adenylyl-sulfate kinase 2, chloroplastic (APK2)
  3. no protein annotated in this organism
This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sulfite from sulfate, the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381Substrate2 Publications
Binding sitei141 – 1411Substrate2 Publications
Sitei150 – 1501Participates in a stacking interaction with the adenine ring of adenylyl-sulfate
Binding sitei155 – 1551Substrate2 Publications
Binding sitei158 – 1581Substrate2 Publications
Active sitei182 – 1821Phosphoserine intermediateBy similarity
Binding sitei231 – 2311Substrate; via carbonyl oxygen2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 1169ATP1 Publication

GO - Molecular functioni

  • adenylylsulfate kinase activity Source: TAIR
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT2G14750-MONOMER.
MetaCyc:AT2G14750-MONOMER.
BRENDAi2.7.1.25. 399.
ReactomeiR-ATH-174362. Transport and synthesis of PAPS.
UniPathwayiUPA00140; UER00205.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylyl-sulfate kinase 1, chloroplastic (EC:2.7.1.25)
Alternative name(s):
ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 1
Adenosine-5'-phosphosulfate kinase 1
Short name:
APS kinase 1
Gene namesi
Name:APK1
Synonyms:AKN1
Ordered Locus Names:At2g14750
ORF Names:F26C24.11, T6B13.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G14750.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions. Apk1 and apk2 double mutant exhibits a semi-dwarf phenotype.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861C → A: Increased catalytic efficiency in oxidative conditions; when associated with Ala-119. 1 Publication
Mutagenesisi119 – 1191C → A: Increased catalytic efficiency in oxidative conditions; when associated with Ala-86. 1 Publication
Mutagenesisi136 – 1361D → A or N: Decreases affinity for substrate and catalytic efficiency. 1 Publication
Mutagenesisi182 – 1821S → C or F: No effect on catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838ChloroplastSequence analysisAdd
BLAST
Chaini39 – 276238Adenylyl-sulfate kinase 1, chloroplasticPRO_0000006635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi86 – 86Interchain (with C-119)1 Publication
Disulfide bondi119 – 119Interchain (with C-86)1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ43295.
PRIDEiQ43295.

PTM databases

iPTMnetiQ43295.

Expressioni

Tissue specificityi

Expressed in root vasculature, root tips, leaf epidermal and guard cells, pollen grains and funiculus of developing seeds.1 Publication

Gene expression databases

GenevisibleiQ43295. AT.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interacts with APK2.3 Publications

Protein-protein interaction databases

DIPiDIP-60003N.
IntActiQ43295. 2 interactions.
STRINGi3702.AT2G14750.1.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi90 – 978Combined sources
Beta strandi102 – 1076Combined sources
Helixi114 – 12714Combined sources
Beta strandi132 – 1365Combined sources
Helixi137 – 1404Combined sources
Turni141 – 1477Combined sources
Helixi152 – 17120Combined sources
Beta strandi175 – 1795Combined sources
Helixi185 – 1939Combined sources
Beta strandi199 – 2057Combined sources
Helixi209 – 2157Combined sources
Helixi220 – 2256Combined sources
Turni233 – 2353Combined sources
Beta strandi246 – 2494Combined sources
Helixi257 – 27115Combined sources
Turni272 – 2743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UIEX-ray1.79A/B/C77-276[»]
4FXPX-ray1.95A/B/C77-276[»]
ProteinModelPortaliQ43295.
SMRiQ43295. Positions 80-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni181 – 1822Substrate binding

Sequence similaritiesi

Belongs to the APS kinase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0635. Eukaryota.
COG0529. LUCA.
HOGENOMiHOG000228204.
KOiK00860.
OMAiKLCYILD.
PhylomeDBiQ43295.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00065. Adenylyl_sulf_kinase.
InterProiIPR002891. APS_kinase.
IPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00455. apsK. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q43295-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAAGAKSLL GLSMASPKGI FDSNSMSNSR SVVVVRACVS MDGSQTLSHN
60 70 80 90 100
KNGSIPEVKS INGHTGQKQG PLSTVGNSTN IKWHECSVEK VDRQRLLDQK
110 120 130 140 150
GCVIWVTGLS GSGKSTLACA LNQMLYQKGK LCYILDGDNV RHGLNRDLSF
160 170 180 190 200
KAEDRAENIR RVGEVAKLFA DAGIICIASL ISPYRTDRDA CRSLLPEGDF
210 220 230 240 250
VEVFMDVPLS VCEARDPKGL YKLARAGKIK GFTGIDDPYE PPLNCEISLG
260 270
REGGTSPIEM AEKVVGYLDN KGYLQA
Length:276
Mass (Da):29,787
Last modified:November 1, 1996 - v1
Checksum:iCB698643AA09D811
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411M → I in AAM62496 (Ref. 7) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75782 mRNA. Translation: CAA53426.1.
U05238 mRNA. Translation: AAC50035.1.
U59759 Genomic DNA. Translation: AAC50034.1.
AC004705 Genomic DNA. Translation: AAC24182.1.
CP002685 Genomic DNA. Translation: AEC06330.1.
AY054287 mRNA. Translation: AAL06946.1.
AY132010 mRNA. Translation: AAM91043.1.
AY085264 mRNA. Translation: AAM62496.1.
PIRiS47640.
RefSeqiNP_179082.1. NM_127039.3.
UniGeneiAt.10821.

Genome annotation databases

EnsemblPlantsiAT2G14750.1; AT2G14750.1; AT2G14750.
GeneIDi815963.
GrameneiAT2G14750.1; AT2G14750.1; AT2G14750.
KEGGiath:AT2G14750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75782 mRNA. Translation: CAA53426.1.
U05238 mRNA. Translation: AAC50035.1.
U59759 Genomic DNA. Translation: AAC50034.1.
AC004705 Genomic DNA. Translation: AAC24182.1.
CP002685 Genomic DNA. Translation: AEC06330.1.
AY054287 mRNA. Translation: AAL06946.1.
AY132010 mRNA. Translation: AAM91043.1.
AY085264 mRNA. Translation: AAM62496.1.
PIRiS47640.
RefSeqiNP_179082.1. NM_127039.3.
UniGeneiAt.10821.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UIEX-ray1.79A/B/C77-276[»]
4FXPX-ray1.95A/B/C77-276[»]
ProteinModelPortaliQ43295.
SMRiQ43295. Positions 80-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60003N.
IntActiQ43295. 2 interactions.
STRINGi3702.AT2G14750.1.

PTM databases

iPTMnetiQ43295.

Proteomic databases

PaxDbiQ43295.
PRIDEiQ43295.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G14750.1; AT2G14750.1; AT2G14750.
GeneIDi815963.
GrameneiAT2G14750.1; AT2G14750.1; AT2G14750.
KEGGiath:AT2G14750.

Organism-specific databases

TAIRiAT2G14750.

Phylogenomic databases

eggNOGiKOG0635. Eukaryota.
COG0529. LUCA.
HOGENOMiHOG000228204.
KOiK00860.
OMAiKLCYILD.
PhylomeDBiQ43295.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00205.
BioCyciARA:AT2G14750-MONOMER.
MetaCyc:AT2G14750-MONOMER.
BRENDAi2.7.1.25. 399.
ReactomeiR-ATH-174362. Transport and synthesis of PAPS.

Miscellaneous databases

PROiQ43295.

Gene expression databases

GenevisibleiQ43295. AT.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00065. Adenylyl_sulf_kinase.
InterProiIPR002891. APS_kinase.
IPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00455. apsK. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cDNA for adenylyl sulphate (APS)-kinase from Arabidopsis thaliana."
    Arz H.E., Gisselmann G., Schiffmann S., Schwenn J.-D.
    Biochim. Biophys. Acta 1218:447-452(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Leaf.
  2. "A cDNA clone for 5'-adenylylphosphosulfate kinase from Arabidopsis thaliana."
    Jain A., Leustek T.
    Plant Physiol. 105:771-772(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "APS kinase from Arabidopsis thaliana: genomic organization, expression, and kinetic analysis of the recombinant enzyme."
    Lee S., Leustek T.
    Biochem. Biophys. Res. Commun. 247:171-175(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "APS-sulfotransferase activity is identical to higher plant APS-kinase (EC 2.7.1.25)."
    Schiffmann S., Schwenn J.D.
    FEBS Lett. 355:229-232(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Molecular and catalytic properties of Arabidopsis thaliana adenylyl sulfate (APS)-kinase."
    Lillig C.H., Schiffmann S., Berndt C., Berken A., Tischka R., Schwenn J.D.
    Arch. Biochem. Biophys. 392:303-310(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH AKN2, MUTAGENESIS OF SER-182.
  10. "Disruption of adenosine-5'-phosphosulfate kinase in Arabidopsis reduces levels of sulfated secondary metabolites."
    Mugford S.G., Yoshimoto N., Reichelt M., Wirtz M., Hill L., Mugford S.T., Nakazato Y., Noji M., Takahashi H., Kramell R., Gigolashvili T., Fluegge U.I., Wasternack C., Gershenzon J., Hell R., Saito K., Kopriva S.
    Plant Cell 21:910-927(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  11. "Adenosine-5'-phosphosulfate kinase is essential for Arabidopsis viability."
    Mugford S.G., Matthewman C.A., Hill L., Kopriva S.
    FEBS Lett. 584:119-123(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "Interaction of glucosinolate content of Arabidopsis thaliana mutant lines and feeding and oviposition by generalist and specialist lepidopterans."
    Badenes-Perez F.R., Reichelt M., Gershenzon J., Heckel D.G.
    Phytochemistry 86:36-43(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Nucleotide binding site communication in Arabidopsis thaliana adenosine 5'-phosphosulfate kinase."
    Ravilious G.E., Jez J.M.
    J. Biol. Chem. 287:30385-30394(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 77-276 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF ASP-136.
  14. "Structural basis and evolution of redox regulation in plant adenosine-5'-phosphosulfate kinase."
    Ravilious G.E., Nguyen A., Francois J.A., Jez J.M.
    Proc. Natl. Acad. Sci. U.S.A. 109:309-314(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 77-276 IN COMPLEX WITH SUBSTRATE AND ATP, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-86 AND CYS-119.

Entry informationi

Entry nameiAPK1_ARATH
AccessioniPrimary (citable) accession number: Q43295
Secondary accession number(s): Q8LES2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.