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Sequence of ATH1_YEAST

EC Number:3.2.1.28

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
alpha,alpha-trehalase
P48016
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1211
136921
Reaction
alpha,alpha-trehalose + H2O = beta-D-glucose + alpha-D-glucose
Other sequences found for EC No. 3.2.1.28

General information:

Sequence
show sequence in fasta format
   0 MKRIRSLWFN AEASYSNLNN SPSLRNKNST GNNSRSKNYR SFSRFDLINS ILLLMMLFLL
  60 AIFVTALYLT KSSRLTYSHA SRAALFNPLG VISPSLGNHT LNYDPEARES SKKLYELLSD
 120 FNTAYYDDEN MILGSNLFSK NTYSRQPYVA NGYIGSRIPN IGFGYALDTL NFYTDAPGAL
 180 NNGWPLRNHR FAGAFVSDFY CLQPKLNSTN FPELDDVGYS TVISSIPQWT NLQFSLVNDS
 240 KWFNPQNVTL DDVTNYSQNL SMKDGIVTTE LDWLNSQIHV KSEIWAHRHI HPLGVVSLEI
 300 SLNTDHLPSD FDSLDVNIWD ILDFNTSHRT VLHSTGTDEK NNAVFMIVQP DNVPSSNCAI
 360 YSTCTVKYEN STNPINSSES FEEKDVSSNI YNVILTEDQP KIIVHKYVGI MSTEFNKNKE
 420 QQDNTNIGLA KMIALNSKGN YEKLLSSHKR AWYDLYNDAF IEIPSDSLLE MTARSSLFHL
 480 LANTRDYNVS SDRGLPVGVS GLSSDSYGGM VFWDADIWME PALLPFFPNV AQNMNNYRNA
 540 THSQAKLNAE KYGYPGAIYP WTSGKYANCT STGPCVDYEY HINVDVAMAS FSIYLNGHEG
 600 IDDEYLRYTT WPIIKNAAQF FTAYVKYNSS LGLYETYNLT DPDEFANHIN NGAFTNAGIK
 660 TLLKWATDIG NHLGEVVDPK WSEISKDIYI PRSSSNITLE YSGMNSSVEI KQADVTLMVY
 720 PLGYINDESI LNNAIKDLYY YSERQSASGP AMTYPVFVAA AAGLLNHGSS SQSYLYKSVL
 780 PYLRAPFAQF SEQSDDNFLT NGLTQPAFPF LTANGGFLQS ILFGLTGIRY SYEVDPDTKK
 840 INRLLRFNPI ELPLLPGGIA IRNFKYMNQV LDIIIDDHNG TIVHKSGDVP IHIKIPNRSL
 900 IHDQDINFYN GSENERKPNL ERRDVDRVGD PMRMDRYGTY YLLKPKQELT VQLFKPGLNA
 960 RNNIAENKQI TNLTAGVPGD VAFSALDGNN YTHWQPLDKI HRAKLLIDLG EYNEKEITKG
1020 MILWGQRPAK NISISILPHS EKVENLFANV TEIMQNSGND QLLNETIGQL LDNAGIPVEN
1080 VIDFDGIEQE DDESLDDVQA LLHWKKEDLA KLIEQIPRLN FLKRKFVKIL DNVPVSPSEP
1140 YYEASRNQSL IEILPSNRTT FTIDYDKLQV GDKGNTDWRK TRYIVVAVQG VYDDYDDDNK
1200 GATIKEIVLN D
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1032077
Destruelle M.,Holzer H.,Klionsky D.J.
Isolation and characterization of a novel yeast gene, ATH1, that is required for vacuolar acid trehalase activity.
Yeast
11
1015-1025
1995
1032078
Bussey H.,Storms R.K.,Ahmed A.,Albermann K.,Allen E.,Ansorge W.,Araujo R.,Aparicio A.,Barrell B.G.,Badcock K.,Benes V.,Botstein D.,Bowman S.,Brueckner M.,Carpenter J.,Cherry J.M.,Chung E.,Churcher C.M.,Coster F.,Davis K.,Davis R.W.,Dietrich F.S.,Delius H.,DiPaolo T.,Dubois E.,Duesterhoeft A.,Duncan M.,Floeth M.,Fortin N.,Friesen J.D.,Fritz C.,Goffeau A.,Hall J.,Hebling U.,Heumann K.,Hilbert H.,Hillier L.W.,Hunicke-Smith S.,Hyman R.W.,Johnston M.,Kalman S.,Kleine K.,Komp C.,Kurdi O.,Lashkari D.,Lew H.,Lin A.,Lin D.,Louis E.J.,Marathe R.,Messenguy F.,Mewes H.-W.,Mirtipati S.,Moestl D.,Mueller-Auer S.,Namath A.,Nentwich U.,Oefner P.,Pearson D.,Petel F.X.,Pohl T.M.,Purnelle B.,Rajandream M.A.,Rechmann S.,Rieger M.,Riles L.,Roberts D.,Schaefer M.,Scharfe M.,Scherens B.,Schramm S.,Schroeder M.,Sdicu A.-M.,Tettelin H.,Urrestarazu L.A.,Ushinsky S.,Vierendeels F.,Vissers S.,Voss H.,Walsh S.V.,Wambutt R.,Wang Y.,Wedler E.,Wedler H.,Winnett E.,Zhong W.-W.,Zollner A.,Vo D.H.,Hani J.
The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.
Nature
387
103-105
1997
1032079
Engel S.R.,Dietrich F.S.,Fisk D.G.,Binkley G.,Balakrishnan R.,Costanzo M.C.,Dwight S.S.,Hitz B.C.,Karra K.,Nash R.S.,Weng S.,Wong E.D.,Lloyd P.,Skrzypek M.S.,Miyasato S.R.,Simison M.,Cherry J.M.
The reference genome sequence of Saccharomyces cerevisiae: Then and now.
G3 (Bethesda)
4
389-398
2014
1032080
Alizadeh P.,Klionsky D.J.
Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae.
FEBS Lett.
391
273-278
1996
1032081
Nwaka S.,Mechler B.,Holzer H.
Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose.
FEBS Lett.
386
235-238
1996
1032082
Huang J.,Reggiori F.,Klionsky D.J.
The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting.
Mol. Biol. Cell
18
2511-2524
2007
1032083
He S.,Bystricky K.,Leon S.,Francois J.M.,Parrou J.L.
The Saccharomyces cerevisiae vacuolar acid trehalase is targeted at the cell surface for its physiological function.
FEBS J.
276
5432-5446
2009