ATDA_VIBCH
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 03-AUG-2022, entry version 109.
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; Proteobacteria; 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 PRIDE; Q9KL03; -.
DR DNASU; 2612395; -.
DR EnsemblBacteria; AAF96843; AAF96843; VC_A0947.
DR GeneID; 57742312; -.
DR KEGG; vch:VC_A0947; -.
DR PATRIC; fig|243277.26.peg.3559; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_013985_3_2_6; -.
DR OMA; IYEAKQL; -.
DR BioCyc; VCHO:VCA0947-MON; -.
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 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 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
