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
SFUM : 130039807(NAA40) 130046104
ACYG : 125181661 136789263
ACHC : 115337567 115338459
ASAO : 132761681 132764426(NAA40)
PGUT : 117670765(NAA40) 132709980 132710793
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
CSAI : 133420406(naa40) 133456345
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
CCOG : 133124444(naa40) 133133008
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
MCAZ : 138027307 138042899
HSYR : 120129420 120134821 120207468
MSYL : 126598787 126624940
SSPL : 121748014 121786299
SMIL : 131020146 131020238
CSIN : 114272833 114315925
PSOM : 113316807 113323159 113328403
DOSA : Os02g0772300 Os05g0387800
TAES : 123128521 123138389 123145642
MFLO : 136464590 136464591 136467844 136467845 136474981
PVIR : 120643423 120657329
SMO : SELMODRAFT_116063 SELMODRAFT_86274
MIS : MICPUN_100333 MICPUN_60060 MICPUN_72973
MPP : MICPUCDRAFT_46969 MICPUCDRAFT_7366
CGR : 2890216(GVI51_K02805)
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)
LBG : 92210392(LODBEIA_P51960)
CAL : CAALFM_C401250WA(NAT4)
CTEN : 18246278(PSN45_001474)
YLI : 2907598(YALI2_B00643g)
NTE : NEUTE1DRAFT102894(NEUTE1DRAFT_102894)
SMP : 10802466(SMAC4_07429)
TATV : 25778258(TrAtP1_006526)
TASP : 36618960(TrAFT101_005790)
PLJ : 28891243(PLICBS_004458)
CDET : 87949177(CDEST_12677)
CPW : 9696106(D8B26_004815)
PTRR : 6340978(PtrM4_063360)
ADAC : 96088336(ACET3X_008014)
CDEP : 91084499(L203_100283)
KMG : 30163073(I203_102065)
KNE : 92180170(IAR55_002912)
CCAC : CcaHIS019_0501560(CcaverHIS019_0501560)
ABV : AGABI2DRAFT239526(AGABI2DRAFT_239526)
PLAG : 39743469(PADL01_1322200)
PBRS : 92372427(MKS88_004340)
TVA : TVAG_2v0254480 TVAG_2v0488670 TVAG_2v0864310 TVAG_2v0899830 TVAG_2v0983850
EHX : EMIHUDRAFT_124867 EMIHUDRAFT_436794
GTT : GUITHDRAFT_101053 GUITHDRAFT_118263 GUITHDRAFT_136122
» 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