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NAA50_XENTR
ID   NAA50_XENTR             Reviewed;         169 AA.
AC   Q5XGA9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=N-alpha-acetyltransferase 50;
DE            EC=2.3.1.258 {ECO:0000250|UniProtKB:Q9GZZ1};
DE   AltName: Full=N-acetyltransferase NAT13;
DE   AltName: Full=N-epsilon-acetyltransferase 50 {ECO:0000250|UniProtKB:Q9GZZ1};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q9GZZ1};
DE   AltName: Full=NatE catalytic subunit;
GN   Name=naa50; Synonyms=nat13;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: N-alpha-acetyltransferase that acetylates the N-terminus of
CC       proteins that retain their initiating methionine. Has a broad substrate
CC       specificity: able to acetylate the initiator methionine of most
CC       peptides, except for those with a proline in second position. Also
CC       displays N-epsilon-acetyltransferase activity by mediating acetylation
CC       of the side chain of specific lysines on proteins. The relevance of N-
CC       epsilon-acetyltransferase activity is however unclear. Required for
CC       sister chromatid cohesion during mitosis by promoting binding of
CC       CDCA5/sororin to cohesin. {ECO:0000250|UniProtKB:Q9GZZ1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein];
CC         Xref=Rhea:RHEA:50564, Rhea:RHEA-COMP:12726, Rhea:RHEA-COMP:12727,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133398, ChEBI:CHEBI:133399; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein];
CC         Xref=Rhea:RHEA:50568, Rhea:RHEA-COMP:12728, Rhea:RHEA-COMP:12729,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133400, ChEBI:CHEBI:133401; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein];
CC         Xref=Rhea:RHEA:50572, Rhea:RHEA-COMP:12730, Rhea:RHEA-COMP:12731,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133402, ChEBI:CHEBI:133403; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA
CC         + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein];
CC         Xref=Rhea:RHEA:50576, Rhea:RHEA-COMP:12732, Rhea:RHEA-COMP:12733,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133404, ChEBI:CHEBI:133405; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:50580, Rhea:RHEA-COMP:12734, Rhea:RHEA-COMP:12735,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133406, ChEBI:CHEBI:133407; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC         H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC         Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC         CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC         [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC         COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC         + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC         Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.258;
CC         Evidence={ECO:0000250|UniProtKB:Q9GZZ1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ1}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9GZZ1}. Note=Localizes to the cytoplasm in
CC       interphase cells. {ECO:0000250|UniProtKB:Q9GZZ1}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC084533; AAH84533.1; -; mRNA.
DR   RefSeq; NP_001011131.1; NM_001011131.1.
DR   AlphaFoldDB; Q5XGA9; -.
DR   SMR; Q5XGA9; -.
DR   STRING; 8364.ENSXETP00000016345; -.
DR   PaxDb; Q5XGA9; -.
DR   GeneID; 496547; -.
DR   KEGG; xtr:496547; -.
DR   CTD; 80218; -.
DR   Xenbase; XB-GENE-996002; naa50.
DR   eggNOG; KOG3138; Eukaryota.
DR   InParanoid; Q5XGA9; -.
DR   OrthoDB; 1536763at2759; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0031415; C:NatA complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0052858; F:peptidyl-lysine acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR   GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; ISS:UniProtKB.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
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; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..169
FT                   /note="N-alpha-acetyltransferase 50"
FT                   /id="PRO_0000284907"
FT   DOMAIN          5..154
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          137..140
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         76..89
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
FT   BINDING         78..89
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..125
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZZ1"
SQ   SEQUENCE   169 AA;  19412 MW;  9DFAF336B97CB15C CRC64;
     MKGRIELGDV TPHNIKQLKR LNQVIFPVSY NDKFYKDVLE VGELAKLAYF NDIAVGAVCC
     RVDHSQNQKR LYIMTLGCLA PYRRLGIGTK MLNHVLNICE KDGTFDNIYL HVQISNESAI
     DFYRKFGFEI IETKKNYYKR IEPADAHVLQ KNLKISSPGQ NADVQKSEN
 
 
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