NAT_SULTO
ID NAT_SULTO Reviewed; 167 AA.
AC Q976C3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=N-alpha-acetyltransferase {ECO:0000250|UniProtKB:Q980R9};
DE Short=NAT {ECO:0000250|UniProtKB:Q980R9};
DE EC=2.3.1.255 {ECO:0000250|UniProtKB:Q980R9};
DE EC=2.3.1.258 {ECO:0000250|UniProtKB:Q980R9};
DE AltName: Full=Amino-terminal acetyltransferase {ECO:0000250|UniProtKB:Q980R9};
DE AltName: Full=N-terminal acetyltransferase {ECO:0000250|UniProtKB:Q980R9};
GN OrderedLocusNames=STK_02580;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Displays alpha (N-terminal) acetyltransferase activity.
CC Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA
CC to the free alpha-amino group at the N-terminus of a protein.
CC {ECO:0000250|UniProtKB:Q980R9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:Q980R9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:Q980R9};
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:Q980R9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133359, ChEBI:CHEBI:133360;
CC Evidence={ECO:0000250|UniProtKB:Q980R9};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q980R9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q980R9}.
CC -!- MISCELLANEOUS: NAT does not require a binding partner for activity.
CC {ECO:0000250|UniProtKB:Q980R9}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000250|UniProtKB:Q980R9}.
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DR EMBL; BA000023; BAB65224.1; -; Genomic_DNA.
DR RefSeq; WP_010978207.1; NC_003106.2.
DR AlphaFoldDB; Q976C3; -.
DR SMR; Q976C3; -.
DR STRING; 273063.STK_02580; -.
DR EnsemblBacteria; BAB65224; BAB65224; STK_02580.
DR GeneID; 42799739; -.
DR KEGG; sto:STK_02580; -.
DR PATRIC; fig|273063.9.peg.309; -.
DR eggNOG; arCOG00833; Archaea.
DR OMA; SGEIMGY; -.
DR OrthoDB; 95090at2157; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0031415; C:NatA complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro.
DR InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR01575; rimI; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW Zinc.
FT CHAIN 1..167
FT /note="N-alpha-acetyltransferase"
FT /id="PRO_0000281645"
FT DOMAIN 12..167
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 92..94
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 100..105
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 132
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 139..141
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT SITE 35
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT SITE 75
FT /note="Plays an important role in modulating multiple
FT conformations of loop regions and contributes to protein
FT thermostability"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT SITE 82
FT /note="Plays an important role in modulating multiple
FT conformations of loop regions and contributes to protein
FT thermostability"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
SQ SEQUENCE 167 AA; 19276 MW; 0498203F042BF9EF CRC64;
MEFAEAKKGK EYRIRNARLT DVDQIIKINR LALPENYPYY FFVEHLKEYE AAFFVAEVDG
EVVGYIMPRI EWGFSNLKQL PTLVKKGHVV SIAVLEQYRR LGIGTALLQA SMKAMKEVYN
AEEVYLEVRV SNSPAINLYK KLGFKEVKVL RHYYADGEDA YLMAAPL
