ID   ATAT_GIAIC              Reviewed;         362 AA.
AC   A8BM50;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=GL50803_16348;
OS   Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=184922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50803 / WB clone C6;
RX   PubMed=17901334; DOI=10.1126/science.1143837;
RA   Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA   Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA   Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA   Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D.,
RA   Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA   Svard S.G., Sogin M.L.;
RT   "Genomic minimalism in the early diverging intestinal parasite Giardia
RT   lamblia.";
RL   Science 317:1921-1926(2007).
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; AACB02000025; EDO78575.1; -; Genomic_DNA.
DR   RefSeq; XP_001706249.1; XM_001706197.1.
DR   AlphaFoldDB; A8BM50; -.
DR   SMR; A8BM50; -.
DR   EnsemblProtists; EDO78575; EDO78575; GL50803_16348.
DR   GeneID; 5699137; -.
DR   KEGG; gla:GL50803_0016348; -.
DR   VEuPathDB; GiardiaDB:GL50803_16348; -.
DR   HOGENOM; CLU_766034_0_0_1; -.
DR   InParanoid; A8BM50; -.
DR   OMA; QNETHEM; -.
DR   OrthoDB; 1001524at2759; -.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0019799; F:tubulin N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071929; P:alpha-tubulin acetylation; IBA:GO_Central.
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; Transferase.
FT   CHAIN           1..362
FT                   /note="Alpha-tubulin N-acetyltransferase"
FT                   /id="PRO_0000402089"
FT   DOMAIN          1..177
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   BINDING         111..124
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   BINDING         147..156
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   SITE            52
FT                   /note="Crucial for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ   SEQUENCE   362 AA;  40672 MW;  E5A6E3F6752E3D97 CRC64;
     MQFGCNVAEA FGLRRSGVVL LTDQSLRSMP LSQQKKVEII LDGMGRGSQA AQGLPSPITS
     LAFIRDSHHF LFLAVDEDQC LGILKGGIKH LFMLDSQNET HEMDAMCCLD FYTHETVQRR
     GIGTRLFRAM ELHTHISAQG WAFDRPSPKL LAFLSKVYDM HDFKAQPNNF LMLDASIRLW
     GAEFKQYRRS KKHYIPDAYL LPETRESEYL GEAELTKRTL IRKSTAVIPQ TKTTQSEDAP
     ARALTADELL SKRSVVLPTA SRTPSLPDQP QSVAAAYMNK RIEGAGPSFE QYMRDHYGAK
     SLIVPSEIQT SLNHSKDSVS QEDMIQRQRQ LDRMAFTLAR EANARGSIHN TVGRGVICGR
     RG