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Protein

ATP sulfurylase 2

Gene

APS2

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

Functioni

Catalytic activityi

ATP + sulfate = diphosphate + adenylyl sulfate.3 Publications

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 1 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.

GO - Molecular functioni

  • adenylylsulfate kinase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • sulfate adenylyltransferase (ATP) activity Source: TAIR

GO - Biological processi

  • cellular response to sulfate starvation Source: UniProtKB
  • hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  • sulfate assimilation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:AT1G19920-MONOMER.
UniPathwayiUPA00140; UER00204.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP sulfurylase 2 (EC:2.7.7.4)
Gene namesi
Name:APS2
Synonyms:ASA1, MET3-1
Ordered Locus Names:At1g19920
ORF Names:F6F9.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G19920.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Cytoplasm, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5656ChloroplastSequence analysisAdd
BLAST
Chaini57 – 476420ATP sulfurylase 2PRO_5000144796Add
BLAST

Proteomic databases

PaxDbiQ43870.
PRIDEiQ43870.

Expressioni

Tissue specificityi

Mostly expressed in leaves or cotyledons.1 Publication

Inductioni

In roots, upon sulfur starvation.1 Publication

Gene expression databases

GenevisibleiQ43870. AT.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi23819. 1 interaction.
IntActiQ43870. 1 interaction.
STRINGi3702.AT1G19920.1.

Structurei

3D structure databases

ProteinModelPortaliQ43870.
SMRiQ43870. Positions 64-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfate adenylyltransferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0636. Eukaryota.
COG2046. LUCA.
HOGENOMiHOG000069045.
InParanoidiQ43870.
KOiK13811.
OMAiHVLAEGW.
PhylomeDBiQ43870.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR025980. ATP-Sase_PUA-like_dom.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR024951. Sulfurylase_cat_dom.
IPR002650. Sulphate_adenylyltransferase.
[Graphical view]
PfamiPF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00339. sopT. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q43870-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLMIRSSYV SHITLFQPRN SKPSSFTNQI SFLSSSNNNP FLNLVYKRNL
60 70 80 90 100
TMQSVSKMTV KSSLIDPDGG ELVELIVPET EIGVKKAESE TMPKVKLNQI
110 120 130 140 150
DLEWVHVISE GWASPLKGFM REDEYLQSLH FNSLRLKNGT FVNMSLPIVL
160 170 180 190 200
AIDDDTKEQI GSSENVALVC PQGDIIGSLR SVEIYKHNKE ERIARTWGTT
210 220 230 240 250
SPGLPYVEEY ITPSGNWLIG GDLEVFEPIK YNDGLDHYRL SPKQLREEFD
260 270 280 290 300
NRQADAVFAF QLRNPVHNGH ALLMNDTRKR LLEMGYKNPV LLLHPLGGFT
310 320 330 340 350
KADDVPLDVR MEQHSKVLED GVLDPKTTIV SIFPSPMHYA GPTEVQWHAK
360 370 380 390 400
ARINAGANFY IVGRDPAGMG HPTEKRDLYD PDHGKRVLSM APGLEKLNIL
410 420 430 440 450
PFRVAAYDTI EKKMAFFDPS RAKEFLFISG TKMRTYARTG ENPPDGFMCP
460 470
SGWNVLVKYY ESLQESEAKQ QAVVSA
Length:476
Mass (Da):53,638
Last modified:November 1, 1996 - v1
Checksum:i119FF1A7C10DE9C8
GO
Isoform 2 (identifier: Q43870-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Note: No experimental confirmation available.
Show »
Length:425
Mass (Da):47,775
Checksum:i64AA3EDB899F113F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti453 – 4531W → R in AAM13048 (PubMed:14593172).Curated
Sequence conflicti453 – 4531W → R in AAN15736 (PubMed:14593172).Curated
Sequence conflicti466 – 4661S → K in AAM63309 (Ref. 8) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151Missing in isoform 2. CuratedVSP_041553Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06276 mRNA. Translation: AAA92351.1.
X79210 mRNA. Translation: CAA55799.1.
U40715 mRNA. Translation: AAC49324.1.
U59737 Genomic DNA. Translation: AAB09471.1.
AC007797 Genomic DNA. Translation: AAG12541.1.
CP002684 Genomic DNA. Translation: AEE29913.1.
AY093049 mRNA. Translation: AAM13048.1.
BT000417 mRNA. Translation: AAN15736.1.
AY086101 mRNA. Translation: AAM63309.1.
PIRiS44943.
RefSeqiNP_564099.1. NM_101847.3. [Q43870-1]
UniGeneiAt.24657.

Genome annotation databases

EnsemblPlantsiAT1G19920.1; AT1G19920.1; AT1G19920. [Q43870-1]
GeneIDi838580.
KEGGiath:AT1G19920.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06276 mRNA. Translation: AAA92351.1.
X79210 mRNA. Translation: CAA55799.1.
U40715 mRNA. Translation: AAC49324.1.
U59737 Genomic DNA. Translation: AAB09471.1.
AC007797 Genomic DNA. Translation: AAG12541.1.
CP002684 Genomic DNA. Translation: AEE29913.1.
AY093049 mRNA. Translation: AAM13048.1.
BT000417 mRNA. Translation: AAN15736.1.
AY086101 mRNA. Translation: AAM63309.1.
PIRiS44943.
RefSeqiNP_564099.1. NM_101847.3. [Q43870-1]
UniGeneiAt.24657.

3D structure databases

ProteinModelPortaliQ43870.
SMRiQ43870. Positions 64-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23819. 1 interaction.
IntActiQ43870. 1 interaction.
STRINGi3702.AT1G19920.1.

Proteomic databases

PaxDbiQ43870.
PRIDEiQ43870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G19920.1; AT1G19920.1; AT1G19920. [Q43870-1]
GeneIDi838580.
KEGGiath:AT1G19920.

Organism-specific databases

TAIRiAT1G19920.

Phylogenomic databases

eggNOGiKOG0636. Eukaryota.
COG2046. LUCA.
HOGENOMiHOG000069045.
InParanoidiQ43870.
KOiK13811.
OMAiHVLAEGW.
PhylomeDBiQ43870.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00204.
BioCyciMetaCyc:AT1G19920-MONOMER.

Miscellaneous databases

PROiQ43870.

Gene expression databases

GenevisibleiQ43870. AT.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR025980. ATP-Sase_PUA-like_dom.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR024951. Sulfurylase_cat_dom.
IPR002650. Sulphate_adenylyltransferase.
[Graphical view]
PfamiPF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00339. sopT. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Adenosine-5'-triphosphate-sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent: nucleotide sequence of two adenosine-5'-triphosphate-sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme."
    Murillo M., Leustek T.
    Arch. Biochem. Biophys. 323:195-204(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, PROBABLE ALTERNATIVE INITIATION.
    Strain: cv. Landsberg erecta.
  2. "A cDNA clone for an ATP-sulfurylase from Arabidopsis thaliana."
    Klonus D., Riesmeier J.W., Willmitzer L.
    Plant Physiol. 107:653-654(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Landsberg erecta.
    Tissue: Seedling.
  3. "Cloning of a cDNA encoded by a member of the Arabidopsis thaliana ATP sulfurylase multigene family. Expression studies in yeast and in relation to plant sulfur nutrition."
    Logan H.M., Cathala N., Grignon C., Davidian J.-C.
    J. Biol. Chem. 271:12227-12233(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY SULFUR STARVATION.
    Strain: cv. Landsberg erecta.
  4. "Functional characterization of a gene encoding a fourth ATP sulfurylase isoform from Arabidopsis thaliana."
    Hatzfeld Y., Lee S., Lee M., Leustek T., Saito K.
    Gene 248:51-58(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  5. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "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.
  8. "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].
  9. "Effect of ATP sulfurylase overexpression in bright yellow 2 tobacco cells. Regulation Of atp sulfurylase and SO4(2-) transport activities."
    Hatzfeld Y., Cathala N., Grignon C., Davidian J.-C.
    Plant Physiol. 116:1307-1313(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
    Strain: cv. Landsberg erecta.
  10. "AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins."
    Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N.
    Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAPS2_ARATH
AccessioniPrimary (citable) accession number: Q43870
Secondary accession number(s): Q8LDB2, Q8RWJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 109 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.