Y1754_ARATH
ID Y1754_ARATH Reviewed; 114 AA.
AC Q9CAQ2; Q2HIN3; Q8LEN2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Acetyltransferase At1g77540;
DE EC=2.3.1.-;
DE AltName: Full=Minimal acetyltransferase;
GN OrderedLocusNames=At1g77540; ORFNames=T5M16.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19329564; DOI=10.1104/pp.109.137703;
RA Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT in vivo subcellular targeting verification indicates novel metabolic and
RT regulatory functions of peroxisomes.";
RL Plant Physiol. 150:125-143(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 12-114 IN COMPLEX WITH COENZYME
RP A, AND FUNCTION.
RX PubMed=17128971; DOI=10.1021/bi0612059;
RA Tyler R.C., Bitto E., Berndsen C.E., Bingman C.A., Singh S., Lee M.S.,
RA Wesenberg G.E., Denu J.M., Phillips G.N. Jr., Markley J.L.;
RT "Structure of Arabidopsis thaliana At1g77540 protein, a minimal
RT acetyltransferase from the COG2388 family.";
RL Biochemistry 45:14325-14336(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 12-114 IN COMPLEX WITH COENZYME
RP A.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
CC -!- FUNCTION: Possesses in vitro histone acetyltransferase activity with
CC histones H3 and H4. {ECO:0000269|PubMed:17128971}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19329564}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51659.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010704; AAG51659.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35991.1; -; Genomic_DNA.
DR EMBL; BT024548; ABD38887.1; -; mRNA.
DR EMBL; AY085337; AAM62568.1; -; mRNA.
DR PIR; H96804; H96804.
DR RefSeq; NP_565157.1; NM_106403.4.
DR PDB; 1XMT; X-ray; 1.15 A; A=13-114.
DR PDB; 2EVN; NMR; -; A=12-114.
DR PDB; 2IL4; X-ray; 2.05 A; A=12-114.
DR PDB; 2Q44; X-ray; 1.15 A; A=13-114.
DR PDB; 2Q4Y; X-ray; 2.06 A; A=12-114.
DR PDBsum; 1XMT; -.
DR PDBsum; 2EVN; -.
DR PDBsum; 2IL4; -.
DR PDBsum; 2Q44; -.
DR PDBsum; 2Q4Y; -.
DR AlphaFoldDB; Q9CAQ2; -.
DR BMRB; Q9CAQ2; -.
DR SMR; Q9CAQ2; -.
DR STRING; 3702.AT1G77540.1; -.
DR iPTMnet; Q9CAQ2; -.
DR PaxDb; Q9CAQ2; -.
DR PRIDE; Q9CAQ2; -.
DR ProteomicsDB; 242535; -.
DR DNASU; 844090; -.
DR EnsemblPlants; AT1G77540.1; AT1G77540.1; AT1G77540.
DR GeneID; 844090; -.
DR Gramene; AT1G77540.1; AT1G77540.1; AT1G77540.
DR KEGG; ath:AT1G77540; -.
DR Araport; AT1G77540; -.
DR TAIR; locus:2204715; AT1G77540.
DR eggNOG; ENOG502S1MA; Eukaryota.
DR HOGENOM; CLU_132888_1_0_1; -.
DR InParanoid; Q9CAQ2; -.
DR OMA; RNPSWNT; -.
DR OrthoDB; 1593361at2759; -.
DR PhylomeDB; Q9CAQ2; -.
DR EvolutionaryTrace; Q9CAQ2; -.
DR PRO; PR:Q9CAQ2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAQ2; baseline and differential.
DR Genevisible; Q9CAQ2; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:TAIR.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045057; Gcn5-rel_NAT.
DR InterPro; IPR031165; GNAT_YJDJ.
DR PANTHER; PTHR31435; PTHR31435; 1.
DR Pfam; PF14542; Acetyltransf_CG; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51729; GNAT_YJDJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Peroxisome; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..114
FT /note="Acetyltransferase At1g77540"
FT /id="PRO_0000220598"
FT DOMAIN 18..106
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 52..55
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 61..66
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 88..89
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 93
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17128971,
FT ECO:0000269|PubMed:17850744"
FT BINDING 97
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:17128971,
FT ECO:0000269|PubMed:17850744"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1XMT"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1XMT"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1XMT"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:1XMT"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1XMT"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1XMT"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1XMT"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:1XMT"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1XMT"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:1XMT"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1XMT"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:1XMT"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2EVN"
SQ SEQUENCE 114 AA; 12855 MW; DB18B8D8DC7C8F26 CRC64;
MTNTAATTEA KMATEPPKIV WNEGKRRFET EDHEAFIEYK MRNNGKVMDL VHTYVPSFKR
GLGLASHLCV AAFEHASSHS ISIIPSCSYV SDTFLPRNPS WKPLIHSEVF KSSI
