SAT_CAEEL
ID SAT_CAEEL Reviewed; 160 AA.
AC O17731;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Thialysine N-epsilon-acetyltransferase {ECO:0000303|PubMed:15283700};
DE EC=2.3.1.- {ECO:0000269|PubMed:15283700};
GN ORFNames=D2023.4 {ECO:0000312|WormBase:D2023.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=15283700; DOI=10.1042/bj20040789;
RA Abo-Dalo B., Ndjonka D., Pinnen F., Liebau E., Lueersen K.;
RT "A novel member of the GCN5-related N-acetyltransferase superfamily from
RT Caenorhabditis elegans preferentially catalyses the N-acetylation of
RT thialysine [S-(2-aminoethyl)-L-cysteine].";
RL Biochem. J. 384:129-137(2004).
CC -!- FUNCTION: Catalyzes the N-acetylation of the amino acid thialysine (S-
CC (2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene
CC group substituted with a sulfur (PubMed:15283700). Substrate
CC specificity: thialysine > O-(2-aminoethyl)-L-serine > S-(2-aminoethyl)-
CC D,L-homocysteine (PubMed:15283700). Does not act on polyamines, such as
CC spermidine and spermine, nor on diamines putrescine and cadaverine
CC (PubMed:15283700). {ECO:0000269|PubMed:15283700}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + S-(2-aminoethyl)-L-cysteine = CoA + H(+) + S-(2-
CC acetamidoethyl)-L-cysteine; Xref=Rhea:RHEA:64804, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:156132,
CC ChEBI:CHEBI:156134; Evidence={ECO:0000269|PubMed:15283700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64805;
CC Evidence={ECO:0000269|PubMed:15283700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + O-(2-aminoethyl)-L-serine = CoA + H(+) + O-(2-
CC acetamidoethyl)-L-serine; Xref=Rhea:RHEA:64808, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:156137,
CC ChEBI:CHEBI:156138; Evidence={ECO:0000269|PubMed:15283700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64809;
CC Evidence={ECO:0000269|PubMed:15283700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + S-(2-aminoethyl)-homocysteine = CoA + H(+) + S-
CC (2-acetamidoethyl)-homocysteine; Xref=Rhea:RHEA:64812,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:156135, ChEBI:CHEBI:156136;
CC Evidence={ECO:0000269|PubMed:15283700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64813;
CC Evidence={ECO:0000269|PubMed:15283700};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.18 mM for thialysine (S-(2-aminoethyl)-L-cysteine)
CC {ECO:0000269|PubMed:15283700};
CC KM=0.56 mM for O-(2-aminoethyl)-L-serine
CC {ECO:0000269|PubMed:15283700};
CC KM=3.7 mM for S-(2-aminoethyl)-D,L-homocysteine
CC {ECO:0000269|PubMed:15283700};
CC KM=6.7 mM for L-lysine {ECO:0000269|PubMed:15283700};
CC KM=1.6 mM for ethylenediamine {ECO:0000269|PubMed:15283700};
CC KM=12.4 mM for diaminopropane {ECO:0000269|PubMed:15283700};
CC KM=5.5 mM for spermidine {ECO:0000269|PubMed:15283700};
CC Note=kcat is 38.5 sec(-1) with thialysine (S-(2-aminoethyl)-L-
CC cysteine) as substrate (PubMed:15283700). kcat is 48.9 sec(-1) with
CC O-(2-aminoethyl)-L-serine as substrate (PubMed:15283700). kcat is
CC 27.7 sec(-1) with S-(2-aminoethyl)-D,L-homocysteine as substrate
CC (PubMed:15283700). kcat is 1.4 sec(-1) with L-lysine as substrate
CC (PubMed:15283700). kcat is 5.8 sec(-1) with ethylenediamine as
CC substrate (PubMed:15283700). kcat is 1.2 sec(-1) with diaminopropane
CC as substrate (PubMed:15283700). kcat is 0.14 sec(-1) with spermidine
CC as substrate (PubMed:15283700). {ECO:0000269|PubMed:15283700};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15283700}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; BX284605; CAB02871.1; -; Genomic_DNA.
DR PIR; T20345; T20345.
DR RefSeq; NP_505978.1; NM_073577.4.
DR AlphaFoldDB; O17731; -.
DR SMR; O17731; -.
DR DIP; DIP-27428N; -.
DR STRING; 6239.D2023.4; -.
DR EPD; O17731; -.
DR PaxDb; O17731; -.
DR PeptideAtlas; O17731; -.
DR EnsemblMetazoa; D2023.4.1; D2023.4.1; WBGene00008408.
DR GeneID; 183946; -.
DR KEGG; cel:CELE_D2023.4; -.
DR UCSC; D2023.4.1; c. elegans.
DR CTD; 183946; -.
DR WormBase; D2023.4; CE09074; WBGene00008408; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_013985_41_2_1; -.
DR InParanoid; O17731; -.
DR OMA; WQFYRVE; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; O17731; -.
DR Reactome; R-CEL-351200; Interconversion of polyamines.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00008408; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA: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 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..160
FT /note="Thialysine N-epsilon-acetyltransferase"
FT /id="PRO_0000451288"
FT DOMAIN 4..159
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 84..86
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 92..97
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 123..126
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 130..133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
SQ SEQUENCE 160 AA; 18647 MW; B2D76C6A13FA6DC1 CRC64;
MKNFEIVTVT PDHAEQLISM IHELAEFEKM KSSVVNTAEK LRKDIENKAV HGFIAFIGEE
PAGMNLFYYA YSTWVGQYLH MEDLYIRPQF RRMGLARTLW KKLAELARDK GIVRLEWAVL
DWNKNAIALY DTVDYVNLTK SEGWFTFRMD GAAINKFADE
