ATDA_WIGBR
ID ATDA_WIGBR Reviewed; 174 AA.
AC P0DKR8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Spermidine N(1)-acetyltransferase {ECO:0000250|UniProtKB:P0A951};
DE Short=SAT {ECO:0000250|UniProtKB:P0A951};
DE EC=2.3.1.57 {ECO:0000250|UniProtKB:P0A951};
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase {ECO:0000250|UniProtKB:P0A951};
DE Short=SSAT {ECO:0000250|UniProtKB:P0A951};
GN Name=speG; Synonyms=WGpWb0002; OrderedLocusNames=WIGBRp0020;
OS Wigglesworthia glossinidia brevipalpis.
OG Plasmid pWb1 (pWig1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
CC -!- FUNCTION: Involved in the protection against polyamine toxicity by
CC regulating their concentration. Catalyzes the transfer of an acetyl
CC group from acetyl coenzyme A (AcCoA) to the primary amino groups of
CC spermidine to yield N(1)- and N(8)-acetylspermidine. It can also use
CC spermine. {ECO:0000250|UniProtKB:P0A951}.
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:0000250|UniProtKB:P0A951};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(1)-acetylspermidine;
CC Xref=Rhea:RHEA:28150, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58324; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:P0A951};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(8)-acetylspermidine;
CC Xref=Rhea:RHEA:28270, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:P0A951};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermine = CoA + H(+) + N(1)-acetylspermine;
CC Xref=Rhea:RHEA:33099, ChEBI:CHEBI:15378, ChEBI:CHEBI:45725,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58101; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:P0A951};
CC -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC {ECO:0000250|UniProtKB:P0A951}.
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000250|UniProtKB:P0A951}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000250|UniProtKB:P0A951}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A951}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AB063523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_011013213.1; NC_003425.1.
DR AlphaFoldDB; P0DKR8; -.
DR SMR; P0DKR8; -.
DR OrthoDB; 1538300at2; -.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR Proteomes; UP000000562; Plasmid pWb1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0006598; P:polyamine catabolic process; ISS:UniProtKB.
DR GO; GO:0046203; P:spermidine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Magnesium; Metal-binding; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..174
FT /note="Spermidine N(1)-acetyltransferase"
FT /id="PRO_0000420405"
FT DOMAIN 8..159
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 31
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 36
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 36
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 44
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 44
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 52..55
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 86..88
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 89..91
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 96..102
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 129..138
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT SITE 86
FT /note="Could be important for selectivity toward long
FT polyamines"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
SQ SEQUENCE 174 AA; 20925 MW; BDF268FADC28D9D1 CRC64;
MVQYLKKIKL RPLERDDLTF IHQLDNNASV MRYWFEEPYE AFVELTDLYD KHIHDQSERR
FIIEYSSYKV GLVELVEINY IHRRAEFQII IDPNYQGKGY AVSATKLAIN YAFSILNLYK
LYLVVDESNE KAIHIYLKLG FIIEGRLIHE FFSNGKYRDV IRMCVFQNNF NNKY
