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Protein

Spermidine N(1)-acetyltransferase

Gene

paiA

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the protection against polyamine toxicity by regulating their concentration. Also could be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine.2 Publications

Catalytic activityi

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.1 Publication

Kineticsi

Kcat is 42 min(-1) for acetyltransferase activity with acetylspermidine as substrate (at pH 8.3). Kcat is 31 min(-1) for acetyltransferase activity with AcCoA as substrate (at pH 8.3).1 Publication

      Sites

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Binding sitei131 – 1311Acetyl-CoA1 Publication
      Binding sitei136 – 1361Acetyl-CoA1 Publication
      Binding sitei140 – 1401Acetyl-CoA1 Publication
      Sitei142 – 1421May have an important role in the acetylation of the polyamineBy similarity

      GO - Molecular functioni

      • diamine N-acetyltransferase activity Source: UniProtKB

      GO - Biological processi

      • negative regulation of sporulation Source: UniProtKB
      Complete GO annotation...

      Keywords - Molecular functioni

      Acyltransferase, Transferase

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Spermidine N(1)-acetyltransferase1 Publication (EC:2.3.1.571 Publication)
      Short name:
      SAT1 Publication
      Alternative name(s):
      GCN5-related N-acetyltransferaseCurated
      Short name:
      GNATCurated
      Protease synthase and sporulation negative regulatory protein PAI 11 Publication
      Gene namesi
      Name:paiA1 Publication
      Ordered Locus Names:Ta0374
      OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
      Taxonomic identifieri273075 [NCBI]
      Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
      Proteomesi
      • UP000001024 Componenti: Chromosome

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 161161Spermidine N(1)-acetyltransferasePRO_0000433397Add
      BLAST

      Interactioni

      Subunit structurei

      Monomer or homodimer.1 Publication

      Protein-protein interaction databases

      STRINGi273075.Ta0374.

      Structurei

      Secondary structure

      1
      161
      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Beta strandi3 – 75Combined sources
      Helixi10 – 123Combined sources
      Helixi13 – 2816Combined sources
      Turni29 – 313Combined sources
      Helixi34 – 4411Combined sources
      Helixi47 – 5812Combined sources
      Beta strandi61 – 7010Combined sources
      Beta strandi73 – 8311Combined sources
      Beta strandi86 – 949Combined sources
      Helixi96 – 983Combined sources
      Helixi101 – 11818Combined sources
      Beta strandi122 – 1287Combined sources
      Helixi132 – 1409Combined sources
      Beta strandi144 – 1485Combined sources
      Beta strandi150 – 1589Combined sources

      3D structure databases

      Select the link destinations:
      PDBei
      RCSB PDBi
      PDBji
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      3F0AX-ray2.50A1-159[»]
      3FIXX-ray2.30A/B/C/D1-159[»]
      3K9UX-ray2.30A/B1-159[»]
      3NE7X-ray2.30A1-159[»]
      ProteinModelPortaliQ9HL57.
      ModBaseiSearch...
      MobiDBiSearch...

      Miscellaneous databases

      EvolutionaryTraceiQ9HL57.

      Family & Domainsi

      Domains and Repeats

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Domaini3 – 160158N-acetyltransferasePROSITE-ProRule annotationAdd
      BLAST

      Region

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Regioni92 – 943Acetyl-CoA-binding1 Publication
      Regioni99 – 1046Acetyl-CoA binding1 Publication

      Sequence similaritiesi

      Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

      Phylogenomic databases

      eggNOGiarCOG00844. Archaea.
      COG0454. LUCA.
      HOGENOMiHOG000142612.
      OMAiARESWKW.

      Family and domain databases

      Gene3Di3.40.630.30. 1 hit.
      InterProiIPR016181. Acyl_CoA_acyltransferase.
      IPR000182. GNAT_dom.
      [Graphical view]
      PfamiPF13673. Acetyltransf_10. 1 hit.
      [Graphical view]
      SUPFAMiSSF55729. SSF55729. 1 hit.
      PROSITEiPS51186. GNAT. 1 hit.
      [Graphical view]

      Sequencei

      Sequence statusi: Complete.

      Q9HL57-1 [UniParc]FASTAAdd to basket

      « Hide

              10         20         30         40         50
      MSIEIRKLSI EDLETLIEVA RESWKWTYAG IYSEEYIESW IREKYSKEKL
      60 70 80 90 100
      LNEIVRSQSN LDILFLGAFA DSTLIGFIEL KIIANKAELL RLYLKPEYTH
      110 120 130 140 150
      KKIGKTLLLE AEKIMKKKGI LECRLYVHRQ NSVGFSFYYK NGFKVEDTDG
      160
      SDFIMEKKYE S
      Length:161
      Mass (Da):18,997
      Last modified:March 1, 2001 - v1
      Checksum:i934050066A9DBA05
      GO

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AL445064 Genomic DNA. Translation: CAC11518.1.
      RefSeqiWP_010900802.1. NC_002578.1.

      Genome annotation databases

      EnsemblBacteriaiCAC11518; CAC11518; CAC11518.
      GeneIDi1455990.
      KEGGitac:Ta0374.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AL445064 Genomic DNA. Translation: CAC11518.1.
      RefSeqiWP_010900802.1. NC_002578.1.

      3D structure databases

      Select the link destinations:
      PDBei
      RCSB PDBi
      PDBji
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      3F0AX-ray2.50A1-159[»]
      3FIXX-ray2.30A/B/C/D1-159[»]
      3K9UX-ray2.30A/B1-159[»]
      3NE7X-ray2.30A1-159[»]
      ProteinModelPortaliQ9HL57.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      STRINGi273075.Ta0374.

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsemblBacteriaiCAC11518; CAC11518; CAC11518.
      GeneIDi1455990.
      KEGGitac:Ta0374.

      Phylogenomic databases

      eggNOGiarCOG00844. Archaea.
      COG0454. LUCA.
      HOGENOMiHOG000142612.
      OMAiARESWKW.

      Miscellaneous databases

      EvolutionaryTraceiQ9HL57.

      Family and domain databases

      Gene3Di3.40.630.30. 1 hit.
      InterProiIPR016181. Acyl_CoA_acyltransferase.
      IPR000182. GNAT_dom.
      [Graphical view]
      PfamiPF13673. Acetyltransf_10. 1 hit.
      [Graphical view]
      SUPFAMiSSF55729. SSF55729. 1 hit.
      PROSITEiPS51186. GNAT. 1 hit.
      [Graphical view]
      ProtoNetiSearch...

      Publicationsi

      « Hide 'large scale' publications
      1. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
        Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
        Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
        Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
      2. "Broad-substrate screen as a tool to identify substrates for bacterial Gcn5-related N-acetyltransferases with unknown substrate specificity."
        Kuhn M.L., Majorek K.A., Minor W., Anderson W.F.
        Protein Sci. 22:222-230(2013) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
      3. "Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production."
        Midwest center for structural genomics (MCSG)
        Proteins 79:2566-2577(2011) [PubMed] [Europe PMC] [Abstract]
        Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-159 IN COMPLEX WITH COENZYME A, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBSTRATE SPECIFICITY.

      Entry informationi

      Entry nameiPAIA_THEAC
      AccessioniPrimary (citable) accession number: Q9HL57
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: June 24, 2015
      Last sequence update: March 1, 2001
      Last modified: May 11, 2016
      This is version 71 of the entry and version 1 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programProkaryotic Protein Annotation Program

      Miscellaneousi

      Keywords - Technical termi

      3D-structure, Complete proteome, Reference proteome

      Documents

      1. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      2. 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.