ID   ATAT_SCHJA              Reviewed;         267 AA.
AC   Q5DD96;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=SJCHGC00609;
OS   Schistosoma japonicum (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16617374; DOI=10.1371/journal.ppat.0020029;
RA   Liu F., Lu J., Hu W., Wang S.-Y., Cui S.-J., Chi M., Yan Q., Wang X.-R.,
RA   Song H.-D., Xu X.-N., Wang J.-J., Zhang X.-L., Zhang X., Wang Z.-Q.,
RA   Xue C.-L., Brindley P.J., McManus D.P., Yang P.-Y., Feng Z., Chen Z.,
RA   Han Z.-G.;
RT   "New perspectives on host-parasite interplay by comparative transcriptomic
RT   and proteomic analyses of Schistosoma japonicum.";
RL   PLoS Pathog. 2:268-281(2006).
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; AY814478; AAW26210.1; -; mRNA.
DR   AlphaFoldDB; Q5DD96; -.
DR   SMR; Q5DD96; -.
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:0048666; P:neuron development; 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   2: Evidence at transcript level;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..267
FT                   /note="Alpha-tubulin N-acetyltransferase"
FT                   /id="PRO_0000402077"
FT   DOMAIN          1..197
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   BINDING         131..144
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   BINDING         167..176
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   SITE            60
FT                   /note="Crucial for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ   SEQUENCE   267 AA;  31011 MW;  621CCAC12523B01C CRC64;
     MDFRAGLENV LQQEVTVIHG EETRKLCIAN NKYLNGKDAD TFRNLAVLLD HLGERSAKAQ
     KLPKPVTSFI KFRNSDQSIF LLSDIPVKKF VILIYMFFRV LGFLKVGRKR LFVHDSKGVC
     VECIPLCILD FYIHESHQRK GYGKKLFDFM LKTENIQPSY LAIDLPSMKM IQFLHKHYHL
     INPIYSPNNF VVYSEFFNNL NNSNYSIVQS KLTTTNCFLK SNSSRIHQNK HNHSIVSNNN
     NNNNNNIIII IIIQNITHHN NQLTIEQ