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Protein

Sulfate adenylyltransferase

Gene

sua1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.UniRule annotation

Catalytic activityi

ATP + sulfate = diphosphate + adenylyl sulfate.UniRule annotation

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sulfite from sulfate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Sulfate adenylyltransferase (sua1)
  2. Adenylyl-sulfate kinase (met14)
  3. Probable phosphoadenosine phosphosulfate reductase (met16)
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)DescriptionActionsGraphical viewLength
Active sitei194UniRule annotation1
Active sitei195UniRule annotation1
Active sitei196UniRule annotation1
Sitei199Transition state stabilizerUniRule annotation1
Binding sitei202SubstrateUniRule annotation1
Sitei202Transition state stabilizerUniRule annotation1
Sitei326Induces change in substrate recognition on ATP bindingUniRule annotation1
Binding sitei329ATP; via amide nitrogenUniRule annotation1
Binding sitei352SubstrateUniRule annotation1
Binding sitei353Substrate; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi192 – 196ATPUniRule annotation5
Nucleotide bindingi287 – 291ATPUniRule annotation5

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • sulfate adenylyltransferase (ATP) activity Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis, Methionine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00140; UER00204.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfate adenylyltransferaseUniRule annotation (EC:2.7.7.4UniRule annotation)
Alternative name(s):
ATP-sulfurylaseUniRule annotation
Sulfate adenylate transferaseUniRule annotation
Short name:
SATUniRule annotation
Gene namesi
Name:sua1
Synonyms:asp1, met3
ORF Names:SPBC27.08c, SPBC28F2.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC27.08c.
PomBaseiSPBC27.08c. sua1.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001059531 – 490Sulfate adenylyltransferaseAdd BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei356Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78937.
PRIDEiP78937.

PTM databases

iPTMnetiP78937.

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.UniRule annotation

Protein-protein interaction databases

BioGridi276950. 14 interactors.
MINTiMINT-4691604.

Structurei

3D structure databases

ProteinModelPortaliP78937.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 165N-terminalUniRule annotationAdd BLAST165
Regioni166 – 390CatalyticUniRule annotationAdd BLAST225
Regioni391 – 490Required for oligomerization; adenylyl-sulfate kinase-likeUniRule annotationAdd BLAST100

Domaini

The oligomerization domain is distantly related to APS kinases, but it is not functional and does not bind APS. It is required for oligomerization of the enzyme, although the oligomerization state has no effect on the catalytic activity of the enzyme.UniRule annotation

Sequence similaritiesi

Belongs to the sulfate adenylyltransferase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000069044.
InParanoidiP78937.
KOiK00958.
OMAiNRVDLEW.
OrthoDBiEOG092C20R5.
PhylomeDBiP78937.

Family and domain databases

CDDicd00517. ATPS. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_03106. Sulf_adenylyltr_euk. 1 hit.
InterProiIPR025980. ATP-Sase_PUA-like_dom.
IPR027417. P-loop_NTPase.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR027535. Sulf_adenylyltr_euk.
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.

Sequencei

Sequence statusi: Complete.

P78937-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKALLKDLN ARDAPLREQL EQEATSLPKI VLSERQFCDV ELILNGGFSP
60 70 80 90 100
LDGFMNQKDY LNVVENLRLS TGEVFPIPIT LDLNESQADS LKAGDRVALL
110 120 130 140 150
DPRDGQTVIA ILTVEDKYTP DKANEAEKVF GANDRAHPAV DYLFGRAGNV
160 170 180 190 200
YVGGKLQAVT PIRHFDFVEY RYSPAQLRSD FQRNNWNRVV AFQTRNPMHR
210 220 230 240 250
AHRELTVRAA KQHGARVLIH PVVGMTKPGD IDHFTRVRVY EAILQRYPKG
260 270 280 290 300
SAKLSLLPLA MRMAGPREAL WHAIIRKNYG ASHFIIGRDH AGPGKNSQGE
310 320 330 340 350
DFYGPYDAQY LVEQYAQEIG ITIVPFQMMT YLPDEDIYKP VDKVEPGTRT
360 370 380 390 400
LNISGTELRR RLRVGANIPE WFSYPEVVAI LRQSYPPKYS QGFVLAVPAT
410 420 430 440 450
SDKLLPSALV SALNEDGRRH VTLLPRLDAI SVFYAQELQR AGAAVVVSLA
460 470 480 490
DADASVKVPA EWTTVNIKPK DSVSEVTFAV LSQLSDEGYL
Length:490
Mass (Da):54,754
Last modified:August 14, 2001 - v2
Checksum:iB831C989E9303D85
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti88A → P in BAA12186 (Ref. 2) Curated1
Sequence conflicti100L → I in BAA12186 (Ref. 2) Curated1
Sequence conflicti366A → D in BAA12186 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF421374 Genomic DNA. Translation: AAN32720.1.
D83992 Genomic DNA. Translation: BAA12186.1.
CU329671 Genomic DNA. Translation: CAB89007.1.
PIRiT40044.
RefSeqiNP_595662.2. NM_001021556.3.

Genome annotation databases

EnsemblFungiiSPBC27.08c.1; SPBC27.08c.1:pep; SPBC27.08c.
GeneIDi2540422.
KEGGispo:SPBC27.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF421374 Genomic DNA. Translation: AAN32720.1.
D83992 Genomic DNA. Translation: BAA12186.1.
CU329671 Genomic DNA. Translation: CAB89007.1.
PIRiT40044.
RefSeqiNP_595662.2. NM_001021556.3.

3D structure databases

ProteinModelPortaliP78937.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276950. 14 interactors.
MINTiMINT-4691604.

PTM databases

iPTMnetiP78937.

Proteomic databases

MaxQBiP78937.
PRIDEiP78937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC27.08c.1; SPBC27.08c.1:pep; SPBC27.08c.
GeneIDi2540422.
KEGGispo:SPBC27.08c.

Organism-specific databases

EuPathDBiFungiDB:SPBC27.08c.
PomBaseiSPBC27.08c. sua1.

Phylogenomic databases

HOGENOMiHOG000069044.
InParanoidiP78937.
KOiK00958.
OMAiNRVDLEW.
OrthoDBiEOG092C20R5.
PhylomeDBiP78937.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00204.

Miscellaneous databases

PROiP78937.

Family and domain databases

CDDicd00517. ATPS. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_03106. Sulf_adenylyltr_euk. 1 hit.
InterProiIPR025980. ATP-Sase_PUA-like_dom.
IPR027417. P-loop_NTPase.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR027535. Sulf_adenylyltr_euk.
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...

Entry informationi

Entry nameiMET3_SCHPO
AccessioniPrimary (citable) accession number: P78937
Secondary accession number(s): Q9P6S1, Q9USV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 14, 2001
Last modified: November 30, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.