ATAT_PLAKH
ID ATAT_PLAKH Reviewed; 184 AA.
AC B3L2R5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Alpha-tubulin N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
DE AltName: Full=Acetyltransferase mec-17 homolog {ECO:0000255|HAMAP-Rule:MF_03130};
GN ORFNames=PKH_072200;
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H;
RX PubMed=18843368; DOI=10.1038/nature07306;
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R.D., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M.A., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clark T.G., Galinski M.R., Hall N., Harper D., Harris D.,
RA Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S., Marti M.,
RA Moule S., Meyer I.M., Ormond D., Peters N., Sanders M., Sanders S.,
RA Sargeant T.J., Simmonds M., Smith F., Squares R., Thurston S., Tivey A.R.,
RA Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F.,
RA Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I.,
RA Barrell B.G., Berriman M.;
RT "The genome of the simian and human malaria parasite Plasmodium knowlesi.";
RL Nature 455:799-803(2008).
CC -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the
CC lumenal side of microtubules. Promotes microtubule destabilization and
CC accelerates microtubule dynamics; this activity may be independent of
CC acetylation activity. Acetylates alpha-tubulin with a slow enzymatic
CC rate, due to a catalytic site that is not optimized for acetyl
CC transfer. Enters the microtubule through each end and diffuses quickly
CC throughout the lumen of microtubules. Acetylates only long/old
CC microtubules because of its slow acetylation rate since it does not
CC have time to act on dynamically unstable microtubules before the enzyme
CC is released. {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-
CC acetyl-L-lysyl-[alpha-tubulin]; Xref=Rhea:RHEA:15277, Rhea:RHEA-
CC COMP:11278, Rhea:RHEA-COMP:11279, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:61930; EC=2.3.1.108; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03130};
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; AM910989; CAQ39291.1; -; Genomic_DNA.
DR RefSeq; XP_002258519.1; XM_002258483.1.
DR AlphaFoldDB; B3L2R5; -.
DR SMR; B3L2R5; -.
DR STRING; 5850.PKH_072200; -.
DR PRIDE; B3L2R5; -.
DR EnsemblProtists; CAQ39291; CAQ39291; PKH_072200.
DR GeneID; 7319972; -.
DR KEGG; pkn:PKNH_0722800; -.
DR VEuPathDB; PlasmoDB:PKNH_0722800; -.
DR HOGENOM; CLU_025013_3_0_1; -.
DR InParanoid; B3L2R5; -.
DR OMA; LCYDNPS; -.
DR PhylomeDB; B3L2R5; -.
DR Proteomes; UP000031513; Chromosome 7.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IEA:UniProtKB-UniRule.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03130; mec17; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR038746; Atat.
DR InterPro; IPR007965; GNAT_ATAT.
DR PANTHER; PTHR12327; PTHR12327; 1.
DR Pfam; PF05301; Acetyltransf_16; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51730; GNAT_ATAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..184
FT /note="Alpha-tubulin N-acetyltransferase"
FT /id="PRO_0000402079"
FT DOMAIN 1..174
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 108..121
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 144..153
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT SITE 50
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ SEQUENCE 184 AA; 21361 MW; 78DE3C106072217A CRC64;
MNIPPEKMHN LEIKKHSRVD LLLLRSSDFH SFRKLQRDVD EMGLLSSTEQ HLSGILTTLD
NITDQDNTLY CLTQEGELIG MLKIGTKRLY LYNGKDLHCR SCACLLDFYI QRNFRKRGLG
LELFNFMLKD KAISPSRLCY DNPSYKLQSF LKKHFSPCAL IKQPNNFVIF AEYFGEPEMG
PFGQ
