NAT_SULAC
ID NAT_SULAC Reviewed; 168 AA.
AC Q4JBG0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Saci_0459;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY79869.1; -; Genomic_DNA.
DR RefSeq; WP_011277371.1; NC_007181.1.
DR AlphaFoldDB; Q4JBG0; -.
DR SMR; Q4JBG0; -.
DR STRING; 330779.Saci_0459; -.
DR EnsemblBacteria; AAY79869; AAY79869; Saci_0459.
DR GeneID; 3474550; -.
DR KEGG; sai:Saci_0459; -.
DR PATRIC; fig|330779.12.peg.456; -.
DR eggNOG; arCOG00833; Archaea.
DR HOGENOM; CLU_013985_23_0_2; -.
DR OMA; SGEIMGY; -.
DR Proteomes; UP000001018; 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..168
FT /note="N-alpha-acetyltransferase"
FT /id="PRO_0000281643"
FT DOMAIN 13..168
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 93..95
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 93..95
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 101..106
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 101..106
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 133
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 140..142
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT SITE 36
FT /note="Plays an important role in substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q980R9"
FT SITE 76
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 83
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 168 AA; 19537 MW; 167A7F64766DCE0B CRC64;
MEITEDSKRK INYQIRLATL SDIDQIIRIN RSALPENYPY YFFVEHLKEY GQAFYVADLE
GEVVGYVMPR IEWGFSNLKH IPSLVRKGHI VSIAVLEPFR KIGVGTSLLQ NSLKAMKDTY
NAEEVYLEVR VTNYPAISLY KKFNFREVKL LKHYYADGED AYLMAAPL
