SAT1_MUSSA
ID SAT1_MUSSA Reviewed; 171 AA.
AC P49431;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Diamine acetyltransferase 1;
DE EC=2.3.1.57 {ECO:0000250|UniProtKB:P21673};
DE AltName: Full=Polyamine N-acetyltransferase 1;
DE AltName: Full=Putrescine acetyltransferase;
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase 1 {ECO:0000303|PubMed:8241266};
DE Short=SSAT {ECO:0000303|PubMed:8241266};
DE Short=SSAT-1;
GN Name=Sat1; Synonyms=Sat;
OS Mus saxicola (Brown spiny mouse) (Rock-loving mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Pyromys.
OX NCBI_TaxID=10094;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8241266; DOI=10.1016/0167-4781(93)90152-4;
RA Fogel-Petrovic M., Kramer D.L., Ganis B., Casero R.A. Jr., Porter C.W.;
RT "Cloning and sequence analysis of the gene and cDNA encoding mouse
RT spermidine/spermine N1-acetyltransferase -- a gene uniquely regulated by
RT polyamines and their analogs.";
RL Biochim. Biophys. Acta 1216:255-264(1993).
CC -!- FUNCTION: Enzyme which catalyzes the acetylation of polyamines.
CC Substrate specificity: norspermidine = spermidine >> spermine > N(1)-
CC acetylspermine. This highly regulated enzyme allows a fine attenuation
CC of the intracellular concentration of polyamines. Also involved in the
CC regulation of polyamine transport out of cells. Also acts on 1,3-
CC diaminopropane and 1,5-diaminopentane. {ECO:0000250|UniProtKB:P21673}.
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:P21673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11117;
CC Evidence={ECO:0000250|UniProtKB:P21673};
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:P21673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28151;
CC Evidence={ECO:0000250|UniProtKB:P21673};
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:P21673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33100;
CC Evidence={ECO:0000250|UniProtKB:P21673};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; N-
CC acetylputrescine from putrescine: step 1/1.
CC {ECO:0000250|UniProtKB:P21673}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P21673}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P21673}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; L10245; AAA16567.1; -; Unassigned_DNA.
DR PIR; S43430; S43430.
DR AlphaFoldDB; P49431; -.
DR SMR; P49431; -.
DR MGI; MGI:98233; Sat1.
DR UniPathway; UPA00188; UER00363.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019809; F:spermidine binding; IBA:GO_Central.
DR GO; GO:0006596; P:polyamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032918; P:spermidine acetylation; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032957; SAT1.
DR PANTHER; PTHR10545:SF36; PTHR10545:SF36; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..171
FT /note="Diamine acetyltransferase 1"
FT /id="PRO_0000074594"
FT DOMAIN 4..170
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 27..28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 94..96
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 102..107
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 133..136
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 140..143
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
SQ SEQUENCE 171 AA; 19997 MW; 30125A9F7AA81888 CRC64;
MAKFKIRPAT ASDCSDILRL IKELAKYEYM EDQVILTEKD LLEDGFGEHP FYHCLVAEVP
KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMKC
RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMAAE E
