ID   ATAT_LEIIN              Reviewed;         246 AA.
AC   A4I1F7;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=LinJ25.1190, LinJ_25_1190;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5;
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(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; FR796457; CAM68587.1; -; Genomic_DNA.
DR   RefSeq; XP_001466148.1; XM_001466111.1.
DR   AlphaFoldDB; A4I1F7; -.
DR   SMR; A4I1F7; -.
DR   STRING; 5671.XP_001466148.1; -.
DR   GeneID; 5069583; -.
DR   KEGG; lif:LINJ_25_1190; -.
DR   VEuPathDB; TriTrypDB:LINF_250017700; -.
DR   eggNOG; KOG4601; Eukaryota.
DR   InParanoid; A4I1F7; -.
DR   OMA; FFIGRHP; -.
DR   Proteomes; UP000008153; Chromosome 25.
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..246
FT                   /note="Alpha-tubulin N-acetyltransferase"
FT                   /id="PRO_0000402083"
FT   DOMAIN          21..202
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   BINDING         135..148
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   BINDING         172..181
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   SITE            74
FT                   /note="Crucial for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ   SEQUENCE   246 AA;  27135 MW;  E2E2F2C4A1ABC71D CRC64;
     MRRRPAQLTA TKLADEEVPE LTLVPDGVSR WTGADLDALR NAARRGGAEA AQQDLERKLC
     RTIDILGARS QQAQEINTVL TSVARLRENS TFRLYLLTQN HRGVGILKVG VKKLFVTHPV
     TCGLVEVDPL CVLDFYVDES CQRQGYGKTL YSHMLKAEHV SRPEVLAIDR PSNKLLGFLR
     KHYGLAAYTP QVNNFVVFHS FFDHTTVSER GKLLRAPSPA RALPFSSSTN ATAAIGGAKA
     KNWAPG