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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei194 – 1941UniRule annotation
Active sitei195 – 1951UniRule annotation
Active sitei196 – 1961UniRule annotation
Sitei199 – 1991Transition state stabilizerUniRule annotation
Binding sitei202 – 2021SubstrateUniRule annotation
Sitei202 – 2021Transition state stabilizerUniRule annotation
Sitei326 – 3261Induces change in substrate recognition on ATP bindingUniRule annotation
Binding sitei329 – 3291ATP; via amide nitrogenUniRule annotation
Binding sitei352 – 3521SubstrateUniRule annotation
Binding sitei353 – 3531Substrate; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 1965ATPUniRule annotation
Nucleotide bindingi287 – 2915ATPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • cysteine biosynthetic process Source: UniProtKB-KW
  • hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  • methionine biosynthetic process Source: UniProtKB-KW
  • sulfate assimilation Source: PomBase
  • sulfate assimilation via adenylyl sulfate reduction Source: PomBase
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Sulfate adenylyltransferasePRO_0000105953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei356 – 3561Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78937.

PTM databases

iPTMnetiP78937.

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.UniRule annotation

Protein-protein interaction databases

BioGridi276950. 14 interactions.
MINTiMINT-4691604.

Structurei

3D structure databases

ProteinModelPortaliP78937.
SMRiP78937. Positions 4-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 165165N-terminalUniRule annotationAdd
BLAST
Regioni166 – 390225CatalyticUniRule annotationAdd
BLAST
Regioni391 – 490100Required for oligomerization; adenylyl-sulfate kinase-likeUniRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881A → P in BAA12186 (Ref. 2) Curated
Sequence conflicti100 – 1001L → I in BAA12186 (Ref. 2) Curated
Sequence conflicti366 – 3661A → D in BAA12186 (Ref. 2) Curated

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.
SMRiP78937. Positions 4-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276950. 14 interactions.
MINTiMINT-4691604.

PTM databases

iPTMnetiP78937.

Proteomic databases

MaxQBiP78937.

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: September 7, 2016
This is version 126 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.