ATAT_LEIMA
ID ATAT_LEIMA Reviewed; 246 AA.
AC Q4Q9X8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=LmjF25.1150, LmjF_25_1150;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
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; FR796421; CAJ05171.1; -; Genomic_DNA.
DR RefSeq; XP_001683870.1; XM_001683818.1.
DR AlphaFoldDB; Q4Q9X8; -.
DR SMR; Q4Q9X8; -.
DR STRING; 5664.LmjF.25.1150; -.
DR EnsemblProtists; CAJ05171; CAJ05171; LMJF_25_1150.
DR GeneID; 5652526; -.
DR KEGG; lma:LMJF_25_1150; -.
DR VEuPathDB; TriTrypDB:LmjF.25.1150; -.
DR VEuPathDB; TriTrypDB:LMJLV39_250018300; -.
DR VEuPathDB; TriTrypDB:LMJSD75_250018200; -.
DR eggNOG; KOG4601; Eukaryota.
DR InParanoid; Q4Q9X8; -.
DR OMA; FFIGRHP; -.
DR Proteomes; UP000000542; Chromosome 25.
DR GO; GO:0097014; C:ciliary plasm; ISO:GeneDB.
DR GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0031981; C:nuclear lumen; ISO:GeneDB.
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; Reference proteome; Transferase.
FT CHAIN 1..246
FT /note="Alpha-tubulin N-acetyltransferase"
FT /id="PRO_0000402084"
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; 27203 MW; F3032D6141E163DA CRC64;
MRRRPPQLTK TKLADEEVPE LTLVPDGVSR WTGSDLDALL NAARRGGAEA AQQDLERKLC
RTIDILGARS QQAQEINAVL TSVARLRENS TFRLYLLTQN HRGVGILKVG VKKLFVTHPV
TCGLVEVDPL CVLDFYVDES CQRQGYGKML YSHMLKAEHV SRPEVLAIDR PSNKLLGFLR
KHYGLAAYTP QVNNFVVFHS FFDHTTVSER GKLLRAPSPA RASPFPSSAN ATVAIGGAKA
KNWTPG
