Entry
Name
N-terminal L-serine Nalpha-acetyltransferase NatD;
NAA40 (gene name)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname
acetyl-CoA:N-terminal-L-seryl-[histone 4/2A] L-serine Nalpha-acetyltransferase
Reaction(IUBMB)
(1) acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H4] + CoA;
(2) acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H2A] + CoA
Substrate
acetyl-CoA [CPD:
C00024 ];
N-terminal-L-seryl-[histone H4];
N-terminal-L-seryl-[histone H2A]
Product
N-terminal-Nalpha-acetyl-L-seryl-[histone H4];
CoA [CPD:
C00010 ];
N-terminal-Nalpha-acetyl-L-seryl-[histone H2A]
Comment
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4. Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus.
History
EC 2.3.1.257 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.257
Orthology
K20794 N-alpha-acetyltransferase 40
Genes
MCF : 102132995 102140277(NAA40)
MTHB : 126935594 126941197
ACHC : 115337567 115338459
ASAO : 132761681 132764426(NAA40)
XLA : 108715148(naa40.S) 414673(naa40.L)
DRE : 101882407 550325(naa40)
SANH : 107668433 107691908
SGH : 107562113(naa40) 107588221
CCAR : 109093058 109093074
CAUA : 113052096 113105837
CGIB : 127961152 128017106
MASI : 127414903 127445161
AOCE : 111568559 111583096(naa40)
SASA : 106578099(naa40) 106609028
STRU : 115194695 115198622
OGO : 124008273(naa40) 124013586
OKI : 109896841 109906304(naa40)
OKE : 118369206(naa40) 118392765
SALP : 111951742 112071458
SNH : 120036528(naa40) 120049828
CCLU : 121554363(naa40) 121571244
SFM : 108920268(naa40) 108925397
AANG : 118223371(naa40) 118236359
ARUT : 117398635 117969044
LPIC : 129265111 129283518
DSI : Dsimw501_GD17683(Dsim_GD17683)
ACOZ : 120954828 120959915
AARA : 120902230 120902522
AMER : 121597292 121597628
ASTE : 118510012 118512617
AMOU : 128300717 128303858
AALI : 118461916 118468383
AALB : 109422944 115260596
MSEX : 115450213 119191565
DPL : KGM_214586 KGM_214587
EAF : 111695096 111700859 111714048
PPOI : 119089406 119089660 119114892
CEL : CELE_Y38A10A.7(Y38A10A.7)
PMAX : 117323849 117323850
DPOL : 127856950 127856952
HSYR : 120129420 120134821 120207468
LJA : Lj2g3v0635690.1(Lj2g3v0635690.1) Lj2g3v0635690.2(Lj2g3v0635690.2)
MSYL : 126598787 126624940
SSPL : 121748014 121786299
SMIL : 131020146 131020238
CSIN : 114272833 114315925
PSOM : 113316807 113323159 113328403
DOSA : Os02t0772300-01(Os02g0772300) Os05t0387800-01(Os05g0387800)
TAES : 123128521 123138389 123145642
PVIR : 120643423 120657329
SMO : SELMODRAFT_116063 SELMODRAFT_86274
MIS : MICPUN_100333 MICPUN_60060 MICPUN_72973
MPP : MICPUCDRAFT_46969(JGI:MicpuC2_46969) MICPUCDRAFT_7366(JGI:MicpuC2_7366)
NCS : NCAS_0D02640(NCAS0D02640)
NDI : NDAI_0I02270(NDAI0I02270)
TPF : TPHA_0C04180(TPHA0C04180)
TBL : TBLA_0G02220(TBLA0G02220)
TDL : TDEL_0A03060(TDEL0A03060)
KAF : KAFR_0A01850(KAFR0A01850)
KNG : KNAG_0C05820(KNAG0C05820)
CAL : CAALFM_C401250WA(NAT4)
NTE : NEUTE1DRAFT102894(NEUTE1DRAFT_102894)
CCAC : CcaHIS019_0501560(CcaverHIS019_0501560)
ABV : AGABI2DRAFT239526(AGABI2DRAFT_239526)
EHX : EMIHUDRAFT_124867 EMIHUDRAFT_436794
GTT : GUITHDRAFT_101053 GUITHDRAFT_118263 GUITHDRAFT_136122
TVA : TVAG_2v0254480 TVAG_2v0488670 TVAG_2v0864310 TVAG_2v0899830 TVAG_2v0983850
» show all
Taxonomy
Reference
Authors
Song OK, Wang X, Waterborg JH, Sternglanz R
Title
An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.
Journal
Sequence
Reference
Authors
Polevoda B, Hoskins J, Sherman F
Title
Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.
Journal
Reference
Authors
Magin RS, Liszczak GP, Marmorstein R
Title
The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 2.3.1.257