MAK3_ARATH
ID MAK3_ARATH Reviewed; 190 AA.
AC O80438;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=N-alpha-acetyltransferase MAK3;
DE EC=2.3.1.256 {ECO:0000303|PubMed:12897255};
DE AltName: Full=N-acetyltransferase MAK3 homolog;
DE Short=AtMAK3;
DE AltName: Full=Protein PHOTOSYNTHESIS ALTERED MUTANT 21;
GN Name=MAK3; Synonyms=PAM21; OrderedLocusNames=At2g38130; ORFNames=F16M14.6;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12897255; DOI=10.1105/tpc.012377;
RA Pesaresi P., Gardner N.A., Masiero S., Dietzmann A., Eichacker L.,
RA Wickner R., Salamini F., Leister D.;
RT "Cytoplasmic N-terminal protein acetylation is required for efficient
RT photosynthesis in Arabidopsis.";
RL Plant Cell 15:1817-1832(2003).
CC -!- FUNCTION: Probably required for N-acetylation of some chloroplast
CC precursor proteins and efficient accumulation of thylakoid multiprotein
CC complexes. In yeast, can replace the NatC complex (composed of MAK3,
CC MAK10 and MAK31) by acetylating N termini of endogenous proteins and
CC the N-terminus Met of L-A virus Gag protein. However, the formation of
CC a NatC complex is not required for this function.
CC {ECO:0000269|PubMed:12897255}.
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=2.3.1.256;
CC Evidence={ECO:0000303|PubMed:12897255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-
CC [protein]; Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA-
CC COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256;
CC Evidence={ECO:0000303|PubMed:12897255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256;
CC Evidence={ECO:0000303|PubMed:12897255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-
CC [protein]; Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA-
CC COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256;
CC Evidence={ECO:0000303|PubMed:12897255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256;
CC Evidence={ECO:0000303|PubMed:12897255};
CC -!- INTERACTION:
CC O80438; Q9SZJ6: AGL21; NbExp=3; IntAct=EBI-15205450, EBI-621986;
CC O80438; Q9FG01: ATO; NbExp=3; IntAct=EBI-15205450, EBI-4475455;
CC O80438; A9LNK9: CPSF30; NbExp=3; IntAct=EBI-15205450, EBI-962511;
CC O80438; Q93Z00: TCP14; NbExp=4; IntAct=EBI-15205450, EBI-4424563;
CC O80438; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15205450, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12897255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:12897255}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size and pale-green leaves due to
CC decreased chlorophyll concentration. {ECO:0000269|PubMed:12897255}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily.
CC {ECO:0000305}.
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DR EMBL; AC003028; AAC27162.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09492.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09493.1; -; Genomic_DNA.
DR EMBL; BT010841; AAR24208.1; -; mRNA.
DR EMBL; BT012615; AAT06434.1; -; mRNA.
DR EMBL; AK229007; BAF00894.1; -; mRNA.
DR PIR; T01245; T01245.
DR RefSeq; NP_181348.1; NM_129369.6.
DR RefSeq; NP_973629.1; NM_201900.2.
DR AlphaFoldDB; O80438; -.
DR SMR; O80438; -.
DR BioGRID; 3735; 20.
DR IntAct; O80438; 20.
DR STRING; 3702.AT2G38130.1; -.
DR PaxDb; O80438; -.
DR PRIDE; O80438; -.
DR ProteomicsDB; 239040; -.
DR DNASU; 818391; -.
DR EnsemblPlants; AT2G38130.1; AT2G38130.1; AT2G38130.
DR EnsemblPlants; AT2G38130.2; AT2G38130.2; AT2G38130.
DR GeneID; 818391; -.
DR Gramene; AT2G38130.1; AT2G38130.1; AT2G38130.
DR Gramene; AT2G38130.2; AT2G38130.2; AT2G38130.
DR KEGG; ath:AT2G38130; -.
DR Araport; AT2G38130; -.
DR TAIR; locus:2042867; AT2G38130.
DR eggNOG; KOG3139; Eukaryota.
DR HOGENOM; CLU_013985_0_2_1; -.
DR InParanoid; O80438; -.
DR OMA; HELSEPY; -.
DR OrthoDB; 1323575at2759; -.
DR PhylomeDB; O80438; -.
DR PRO; PR:O80438; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80438; baseline and differential.
DR Genevisible; O80438; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0031417; C:NatC complex; IBA:GO_Central.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR044542; NAA30-like.
DR PANTHER; PTHR45896; PTHR45896; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..190
FT /note="N-alpha-acetyltransferase MAK3"
FT /id="PRO_0000423402"
FT DOMAIN 16..164
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 190 AA; 22123 MW; 124B2D9D44D0A491 CRC64;
MEKEMEDKEE FDEGEIEYTS YAGEHHLPLI MSLVDQELSE PYSIFTYRYF VYLWPQLCFL
AFHKGKCVGT IVCKMGDHRQ TFRGYIAMLV VIKPYRGRGI ASELVTRAIK AMMESGCEEV
TLEAEVSNKG ALALYGRLGF IRAKRLYHYY LNGMDAFRLK LLFPKPRVPQ IPSQVQTQQE
YETFPRPRVP
