ID F6T534_ORNAN Unreviewed; 171 AA.
AC F6T534;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Diamine acetyltransferase 1 {ECO:0000256|ARBA:ARBA00017209};
DE EC=2.3.1.57 {ECO:0000256|ARBA:ARBA00013209};
DE AltName: Full=Polyamine N-acetyltransferase 1 {ECO:0000256|ARBA:ARBA00031435};
DE AltName: Full=Putrescine acetyltransferase {ECO:0000256|ARBA:ARBA00029790};
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase 1 {ECO:0000256|ARBA:ARBA00031532};
GN Name=SAT1 {ECO:0000313|Ensembl:ENSOANP00000018230.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000018230.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000018230.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018230.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000018230.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018230.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023565};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11117;
CC Evidence={ECO:0000256|ARBA:ARBA00023565};
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:0000256|ARBA:ARBA00023509};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28151;
CC Evidence={ECO:0000256|ARBA:ARBA00023509};
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:0000256|ARBA:ARBA00023533};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33100;
CC Evidence={ECO:0000256|ARBA:ARBA00023533};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; N-
CC acetylputrescine from putrescine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004995}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008694}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F6T534; -.
DR STRING; 9258.ENSOANP00000018230; -.
DR Ensembl; ENSOANT00000018233.3; ENSOANP00000018230.3; ENSOANG00000011507.3.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_013985_41_1_1; -.
DR InParanoid; F6T534; -.
DR OMA; DWNEPSI; -.
DR OrthoDB; 722999at2759; -.
DR TreeFam; TF319736; -.
DR UniPathway; UPA00188; UER00363.
DR Proteomes; UP000002279; Chromosome 15.
DR Bgee; ENSOANG00000011507; Expressed in liver and 8 other cell types or tissues.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032918; P:spermidine acetylation; IBA:GO_Central.
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; PTHR10545:SF36; DIAMINE ACETYLTRANSFERASE 1; 1.
DR PANTHER; PTHR10545; DIAMINE N-ACETYLTRANSFERASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002279}.
FT DOMAIN 4..166
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 171 AA; 19970 MW; DF6D4677B49CC8E5 CRC64;
MANFLIRPAG PADCPHILRL IKELAKYEDM EAQVMLTEKD LLEDGFGERP LYHCLVAEVP
EEHWTEEGYG IVGFAMYYFT YDPWIGKLLY LEDFFVMKDF RGFGIGSEIL KNLSQVAVDC
RCSSMHFLVA EWNEPSIEFY KRRGAADLSR EEGWRLFKID KEYLLKMASE E
//
