ID   ATDA_VIBCH              Reviewed;         173 AA.
AC   Q9KL03;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Spermidine N(1)-acetyltransferase {ECO:0000303|PubMed:25623305};
DE            Short=SAT {ECO:0000303|PubMed:25623305};
DE            EC=2.3.1.57 {ECO:0000269|PubMed:25623305};
DE   AltName: Full=Spermidine/spermine N(1)-acetyltransferase {ECO:0000303|PubMed:23184347};
DE            Short=SSAT {ECO:0000303|PubMed:23184347};
GN   Name=speG; OrderedLocusNames=VC_A0947;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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:4MJ8}
RP   X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH SPERMINE.
RA   Filippova E.V., Minasov G., Shuvalova L., Kiryukhina O., Kuhn M.L.,
RA   Anderson W.F.;
RT   "Crystal structure of spermidine N-acetyltransferase from Vibrio cholerae
RT   in complex with polyamine.";
RL   Submitted (SEP-2013) to the PDB data bank.
RN   [4] {ECO:0007744|PDB:4JJX, ECO:0007744|PDB:4MHD, ECO:0007744|PDB:4MI4, ECO:0007744|PDB:4NCZ, ECO:0007744|PDB:4R57, ECO:0007744|PDB:4R87}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND
RP   CALCIUM, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, SUBUNIT, SUBSTRATE SPECIFICITY, AND REACTION
RP   MECHANISM.
RX   PubMed=25623305; DOI=10.1016/j.jmb.2015.01.009;
RA   Filippova E.V., Kuhn M.L., Osipiuk J., Kiryukhina O., Joachimiak A.,
RA   Ballicora M.A., Anderson W.F.;
RT   "A novel polyamine allosteric site of SpeG from Vibrio cholerae is revealed
RT   by its dodecameric structure.";
RL   J. Mol. Biol. 427:1316-1334(2015).
RN   [5] {ECO:0007744|PDB:4JLY, ECO:0007744|PDB:4YGO, ECO:0007744|PDB:5CNP}
RP   X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP   MAGNESIUM, AND SUBUNIT.
RX   PubMed=26410587; DOI=10.1016/j.jmb.2015.09.013;
RA   Filippova E.V., Weigand S., Osipiuk J., Kiryukhina O., Joachimiak A.,
RA   Anderson W.F.;
RT   "Substrate-induced allosteric change in the quaternary structure of the
RT   spermidine N-acetyltransferase SpeG.";
RL   J. Mol. Biol. 427:3538-3553(2015).
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 use
CC       polyamines such as spermine and N(1)-acetylspermine, but not putrescine
CC       or cadaverine. {ECO:0000269|PubMed:23184347,
CC       ECO:0000269|PubMed:25623305}.
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:25623305};
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:0000269|PubMed:25623305};
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:0000269|PubMed:25623305};
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:0000269|PubMed:25623305};
CC   -!- ACTIVITY REGULATION: Allosterically regulated by polyamines
CC       (PubMed:25623305, PubMed:26410587). Polyamines trigger conformational
CC       changes and induce the symmetric closed dodecameric state of the
CC       protein when they bind to their allosteric sites (PubMed:26410587).
CC       {ECO:0000269|PubMed:25623305, ECO:0000269|PubMed:26410587}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=99 uM for spermine (in the presence of 100 uM AcCoA at pH 9 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:25623305};
CC         KM=554 uM for spermidine (in the presence of 100 uM AcCoA at pH 9 and
CC         37 degrees Celsius) {ECO:0000269|PubMed:25623305};
CC         KM=1210 uM for AcCoA (in the presence of 3 mM spermine at pH 9 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:25623305};
CC         Vmax=48.1 umol/min/mg enzyme with AcCoA as substrate (in the presence
CC         of 500 uM spermine at pH 9 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:25623305};
CC         Vmax=19.4 umol/min/mg enzyme with spermine as substrate (in the
CC         presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:25623305};
CC         Vmax=18.8 umol/min/mg enzyme with spermidine as substrate (in the
CC         presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:25623305};
CC         Note=kcat is 16.8 sec(-1) for acetyltransferase activity with AcCoA
CC         as substrate (in the presence of 500 uM spermine at pH 9 and 37
CC         degrees Celsius). kcat is 6.79 sec(-1) for acetyltransferase activity
CC         with spermine as substrate (in the presence of 100 uM AcCoA at pH 9
CC         and 37 degrees Celsius). kcat is 6.58 sec(-1) for acetyltransferase
CC         activity with spermidine as substrate (in the presence of 100 uM
CC         AcCoA at pH 9 and 37 degrees Celsius). {ECO:0000269|PubMed:25623305};
CC   -!- PATHWAY: Amine and polyamine degradation; spermidine degradation.
CC       {ECO:0000305}.
CC   -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Homododecamer; dimer of hexamers (PubMed:25623305,
CC       PubMed:26410587). Exists in solution in a variety of protein
CC       homooligomeric states including dodecamers in an open state. The
CC       presence of the polyamines spermidine or spermine shifts the
CC       equilibrium to dodecamers and induces the formation of the closed,
CC       symmetric dodecamers (PubMed:26410587). {ECO:0000269|PubMed:25623305,
CC       ECO:0000269|PubMed:26410587}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; AE003853; AAF96843.1; -; Genomic_DNA.
DR   PIR; B82398; B82398.
DR   RefSeq; NP_233331.1; NC_002506.1.
DR   RefSeq; WP_001088091.1; NZ_LT906615.1.
DR   PDB; 4JJX; X-ray; 2.83 A; A/B/C=1-173.
DR   PDB; 4JLY; X-ray; 2.88 A; A/B/C/D/E/F=1-173.
DR   PDB; 4MHD; X-ray; 2.32 A; A/B/C=1-173.
DR   PDB; 4MI4; X-ray; 1.85 A; A/B/C=1-173.
DR   PDB; 4MJ8; X-ray; 2.04 A; A/B/C=1-173.
DR   PDB; 4NCZ; X-ray; 1.89 A; A/B/C=1-173.
DR   PDB; 4R57; X-ray; 2.08 A; A/B/C/D/E/F/G/H/I/J/K/L=1-173.
DR   PDB; 4R87; X-ray; 2.61 A; A/B/C/D/E/F/G/H/I/J/K/L=1-173.
DR   PDB; 4YGO; X-ray; 2.50 A; A/B/C/D/E/F=1-173.
DR   PDB; 5CNP; X-ray; 2.38 A; A/B/C/D/E/F=1-173.
DR   PDB; 5UG4; X-ray; 2.15 A; A/B/C=1-173.
DR   PDB; 6CX8; X-ray; 2.41 A; A/B/C/D/E/F=1-173.
DR   PDB; 6DAU; X-ray; 2.26 A; A/B/C/D/E/F=1-173.
DR   PDB; 6E1X; X-ray; 1.35 A; A/B/C/D/E/F=1-173.
DR   PDB; 7KWH; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-173.
DR   PDB; 7KWJ; X-ray; 2.58 A; A/B/C=1-173.
DR   PDB; 7KWQ; X-ray; 2.30 A; A/B/C=1-173.
DR   PDB; 7KWX; X-ray; 2.42 A; A/B/C=1-173.
DR   PDB; 7KX2; X-ray; 2.60 A; A/B/C=1-173.
DR   PDB; 7KX3; X-ray; 2.67 A; A/B/C=1-173.
DR   PDBsum; 4JJX; -.
DR   PDBsum; 4JLY; -.
DR   PDBsum; 4MHD; -.
DR   PDBsum; 4MI4; -.
DR   PDBsum; 4MJ8; -.
DR   PDBsum; 4NCZ; -.
DR   PDBsum; 4R57; -.
DR   PDBsum; 4R87; -.
DR   PDBsum; 4YGO; -.
DR   PDBsum; 5CNP; -.
DR   PDBsum; 5UG4; -.
DR   PDBsum; 6CX8; -.
DR   PDBsum; 6DAU; -.
DR   PDBsum; 6E1X; -.
DR   PDBsum; 7KWH; -.
DR   PDBsum; 7KWJ; -.
DR   PDBsum; 7KWQ; -.
DR   PDBsum; 7KWX; -.
DR   PDBsum; 7KX2; -.
DR   PDBsum; 7KX3; -.
DR   AlphaFoldDB; Q9KL03; -.
DR   SMR; Q9KL03; -.
DR   STRING; 243277.VC_A0947; -.
DR   DNASU; 2612395; -.
DR   EnsemblBacteria; AAF96843; AAF96843; VC_A0947.
DR   GeneID; 69721661; -.
DR   KEGG; vch:VC_A0947; -.
DR   PATRIC; fig|243277.26.peg.3559; -.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_013985_3_2_6; -.
DR   BRENDA; 2.3.1.57; 6626.
DR   UniPathway; UPA00211; -.
DR   UniPathway; UPA00250; -.
DR   EvolutionaryTrace; Q9KL03; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004145; F:diamine N-acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0006598; P:polyamine catabolic process; NAS:UniProtKB.
DR   GO; GO:0046203; P:spermidine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046208; P:spermine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR43415; SPERMIDINE N(1)-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43415:SF3; SPERMIDINE N(1)-ACETYLTRANSFERASE; 1.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Cytoplasm; Magnesium; Metal-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..173
FT                   /note="Spermidine N(1)-acetyltransferase"
FT                   /id="PRO_0000433302"
FT   DOMAIN          5..162
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A951"
FT   BINDING         28
FT                   /ligand="spermine"
FT                   /ligand_id="ChEBI:CHEBI:45725"
FT                   /evidence="ECO:0000269|PubMed:25623305, ECO:0000269|Ref.3,
FT                   ECO:0007744|PDB:4MJ8"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0000269|PubMed:26410587, ECO:0007744|PDB:5CNP"
FT   BINDING         33
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4MHD"
FT   BINDING         33
FT                   /ligand="spermine"
FT                   /ligand_id="ChEBI:CHEBI:45725"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4MI4"
FT   BINDING         41
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4MHD"
FT   BINDING         41
FT                   /ligand="spermine"
FT                   /ligand_id="ChEBI:CHEBI:45725"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4MI4, ECO:0007744|PDB:4R87"
FT   BINDING         49..52
FT                   /ligand="spermine"
FT                   /ligand_id="ChEBI:CHEBI:45725"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4R87"
FT   BINDING         75
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0000269|PubMed:26410587, ECO:0007744|PDB:5CNP"
FT   BINDING         84..86
FT                   /ligand="spermine"
FT                   /ligand_id="ChEBI:CHEBI:45725"
FT                   /evidence="ECO:0000269|PubMed:25623305, ECO:0000269|Ref.3,
FT                   ECO:0007744|PDB:4MJ8"
FT   BINDING         87..89
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4R57, ECO:0007744|PDB:4R87"
FT   BINDING         94..100
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4R57, ECO:0007744|PDB:4R87"
FT   BINDING         127..136
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:25623305,
FT                   ECO:0007744|PDB:4R57"
FT   SITE            84
FT                   /note="Could be important for selectivity toward long
FT                   polyamines"
FT                   /evidence="ECO:0000305|PubMed:25623305"
FT   HELIX           2..4
FT                   /evidence="ECO:0007829|PDB:5CNP"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   HELIX           25..29
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:4NCZ"
FT   HELIX           39..48
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          67..75
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:4R57"
FT   HELIX           99..112
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          140..151
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   STRAND          154..164
FT                   /evidence="ECO:0007829|PDB:6E1X"
FT   HELIX           165..169
FT                   /evidence="ECO:0007829|PDB:6E1X"
SQ   SEQUENCE   173 AA;  20675 MW;  9821218EFF8E8AD8 CRC64;
     MNSQLTLRAL ERGDLRFIHN LNNNRNIMSY WFEEPYESFD ELEELYNKHI HDNAERRFVV
     EDAQKNLIGL VELIEINYIH RSAEFQIIIA PEHQGKGFAR TLINRALDYS FTILNLHKIY
     LHVAVENPKA VHLYEECGFV EEGHLVEEFF INGRYQDVKR MYILQSKYLN RSE
//