ATDA_ECO57
ID ATDA_ECO57 Reviewed; 186 AA.
AC P0A952; P37354;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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; OrderedLocusNames=Z2571, ECs2290;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56571.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35713.1; -; Genomic_DNA.
DR PIR; B90915; B90915.
DR PIR; G85763; G85763.
DR RefSeq; NP_310317.1; NC_002695.1.
DR RefSeq; WP_001138581.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; P0A952; -.
DR SMR; P0A952; -.
DR STRING; 155864.EDL933_2534; -.
DR EnsemblBacteria; AAG56571; AAG56571; Z2571.
DR EnsemblBacteria; BAB35713; BAB35713; ECs_2290.
DR GeneID; 915270; -.
DR KEGG; ece:Z2571; -.
DR KEGG; ecs:ECs_2290; -.
DR PATRIC; fig|386585.9.peg.2398; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_013985_3_2_6; -.
DR OMA; IYEAKQL; -.
DR UniPathway; UPA00211; -.
DR UniPathway; UPA00250; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..186
FT /note="Spermidine N(1)-acetyltransferase"
FT /id="PRO_0000074589"
FT DOMAIN 7..167
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 30
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 35
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 35
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 43
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 43
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 51..54
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 85..87
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 88..90
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 95..101
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT BINDING 128..137
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
FT SITE 85
FT /note="Could be important for selectivity toward long
FT polyamines"
FT /evidence="ECO:0000250|UniProtKB:Q9KL03"
SQ SEQUENCE 186 AA; 21887 MW; 27297083B93B3752 CRC64;
MPSAHSVKLR PLEREDLRYV HQLDNNASVM RYWFEEPYEA FVELSDLYDK HIHDQSERRF
VVECDGEKAG LVELVEINHV HRRAEFQIII SPEYQGKGLA TRAAKLAMDY GFTVLNLYKL
YLIVDKENEK AIHIYRKLGF SVEGELMHEF FINGQYRNAI RMCIFQHQYL AEHKTPGQTL
LKPTAQ
