SAT1_PIG
ID SAT1_PIG Reviewed; 171 AA.
AC Q28999;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
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:8940370};
DE Short=SSAT {ECO:0000303|PubMed:8940370};
DE Short=SSAT-1;
GN Name=SAT1; Synonyms=SAT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endometrium;
RX PubMed=8940370; DOI=10.1210/endo.137.12.8940370;
RA Green M.L., Blaeser L.L., Simmen F.A., Simmen R.C.;
RT "Molecular cloning of spermidine/spermine N1-acetyltransferase from the
RT periimplantation porcine uterus by messenger ribonucleic acid differential
RT display: temporal and conceptus-modulated gene expression.";
RL Endocrinology 137:5447-5455(1996).
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; U57333; AAB50544.1; -; mRNA.
DR RefSeq; NP_999523.1; NM_214358.1.
DR AlphaFoldDB; Q28999; -.
DR SMR; Q28999; -.
DR STRING; 9823.ENSSSCP00000012958; -.
DR PaxDb; Q28999; -.
DR Ensembl; ENSSSCT00005068401; ENSSSCP00005042547; ENSSSCG00005042583.
DR Ensembl; ENSSSCT00045031612; ENSSSCP00045021892; ENSSSCG00045018533.
DR Ensembl; ENSSSCT00055016997; ENSSSCP00055013418; ENSSSCG00055008654.
DR Ensembl; ENSSSCT00065024304; ENSSSCP00065009933; ENSSSCG00065018267.
DR Ensembl; ENSSSCT00070011930; ENSSSCP00070009831; ENSSSCG00070005938.
DR GeneID; 397645; -.
DR KEGG; ssc:397645; -.
DR CTD; 6303; -.
DR eggNOG; KOG3216; Eukaryota.
DR HOGENOM; CLU_013985_41_1_1; -.
DR InParanoid; Q28999; -.
DR OMA; AVERQCG; -.
DR OrthoDB; 1228251at2759; -.
DR TreeFam; TF319736; -.
DR Reactome; R-SSC-351200; Interconversion of polyamines.
DR UniPathway; UPA00188; UER00363.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Genevisible; Q28999; SS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019809; F:spermidine binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..171
FT /note="Diamine acetyltransferase 1"
FT /id="PRO_0000074595"
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; 19893 MW; 531564C4EE91F477 CRC64;
MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP
KEHLTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMKC
RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMAAE E
