PAIA_THEAC
ID PAIA_THEAC Reviewed; 161 AA.
AC Q9HL57;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Spermidine N(1)-acetyltransferase {ECO:0000303|PubMed:21633970};
DE Short=SAT {ECO:0000303|PubMed:21633970};
DE EC=2.3.1.57 {ECO:0000269|PubMed:21633970};
DE AltName: Full=GCN5-related N-acetyltransferase {ECO:0000305};
DE Short=GNAT {ECO:0000305};
DE AltName: Full=Protease synthase and sporulation negative regulatory protein PAI 1 {ECO:0000303|PubMed:21633970};
GN Name=paiA {ECO:0000303|PubMed:21633970}; OrderedLocusNames=Ta0374;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=23184347; DOI=10.1002/pro.2199;
RA Kuhn M.L., Majorek K.A., Minor W., Anderson W.F.;
RT "Broad-substrate screen as a tool to identify substrates for bacterial
RT Gcn5-related N-acetyltransferases with unknown substrate specificity.";
RL Protein Sci. 22:222-230(2013).
RN [3] {ECO:0007744|PDB:3F0A, ECO:0007744|PDB:3FIX, ECO:0007744|PDB:3K9U, ECO:0007744|PDB:3NE7}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-159 IN COMPLEX WITH COENZYME A,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=21633970; DOI=10.1002/prot.23062;
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma
RT acidophilum involved in the negative control of sporulation and degradative
RT enzyme production.";
RL Proteins 79:2566-2577(2011).
CC -!- FUNCTION: Involved in the protection against polyamine toxicity by
CC regulating their concentration. Could also be involved in the negative
CC control of sporulation as well as production of degradative enzymes
CC such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes
CC the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an
CC acceptor substrate and release both CoA and the acetylated product. It
CC can use a variety of substrates including spermidine, L-tryptophan, L-
CC leucine, L-lysine, dopamine and tyramine. {ECO:0000269|PubMed:21633970,
CC ECO:0000269|PubMed:23184347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC ChEBI:CHEBI:70988; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:21633970};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 42 min(-1) for acetyltransferase activity with
CC acetylspermidine as substrate (at pH 8.3). kcat is 31 min(-1) for
CC acetyltransferase activity with AcCoA as substrate (at pH 8.3).
CC {ECO:0000269|PubMed:21633970};
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:21633970}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AL445064; CAC11518.1; -; Genomic_DNA.
DR RefSeq; WP_010900802.1; NC_002578.1.
DR PDB; 3F0A; X-ray; 2.50 A; A=1-159.
DR PDB; 3FIX; X-ray; 2.30 A; A/B/C/D=1-159.
DR PDB; 3K9U; X-ray; 2.30 A; A/B=1-159.
DR PDB; 3NE7; X-ray; 2.30 A; A=1-159.
DR PDBsum; 3F0A; -.
DR PDBsum; 3FIX; -.
DR PDBsum; 3K9U; -.
DR PDBsum; 3NE7; -.
DR AlphaFoldDB; Q9HL57; -.
DR SMR; Q9HL57; -.
DR STRING; 273075.Ta0374; -.
DR EnsemblBacteria; CAC11518; CAC11518; CAC11518.
DR GeneID; 41587478; -.
DR KEGG; tac:Ta0374; -.
DR eggNOG; arCOG00844; Archaea.
DR HOGENOM; CLU_013985_18_3_2; -.
DR OMA; ARESWKW; -.
DR OrthoDB; 83657at2157; -.
DR BRENDA; 2.3.1.57; 6324.
DR EvolutionaryTrace; Q9HL57; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043939; P:negative regulation of sporulation; NAS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..161
FT /note="Spermidine N(1)-acetyltransferase"
FT /id="PRO_0000433397"
FT DOMAIN 3..160
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 92..94
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21633970"
FT BINDING 99..104
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21633970"
FT BINDING 131
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21633970"
FT BINDING 136
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21633970"
FT BINDING 140
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:21633970"
FT SITE 142
FT /note="May have an important role in the acetylation of the
FT polyamine"
FT /evidence="ECO:0000250|UniProtKB:P21340"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3FIX"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3FIX"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:3FIX"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3FIX"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:3FIX"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:3FIX"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:3FIX"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:3FIX"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:3FIX"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3FIX"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3FIX"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:3FIX"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:3FIX"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3FIX"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:3FIX"
SQ SEQUENCE 161 AA; 18997 MW; 934050066A9DBA05 CRC64;
MSIEIRKLSI EDLETLIEVA RESWKWTYAG IYSEEYIESW IREKYSKEKL LNEIVRSQSN
LDILFLGAFA DSTLIGFIEL KIIANKAELL RLYLKPEYTH KKIGKTLLLE AEKIMKKKGI
LECRLYVHRQ NSVGFSFYYK NGFKVEDTDG SDFIMEKKYE S
