Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of CLAT_DROME

EC Number:2.3.1.6

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
choline O-acetyltransferase
P07668
Drosophila melanogaster
721
81328
Reaction
acetyl-CoA + choline = CoA + O-acetylcholine
Other sequences found for EC No. 2.3.1.6

General information:

Sequence
show sequence in fasta format
  0 MASNEASTSA AGSGPESAAL FSKLRSFSIG SGPNSPQRVV SNLRGFLTHR LSNITPSDTG
 60 WKDSILSIPK KWLSTAESVD EFGFPDTLPK VPVPALDETM ADYIRALEPI TTPAQLERTK
120 ELIRQFSAPQ GIGARLHQYL LDKREAEDNW AYYYWLNEMY MDIRIPLPIN SNPGMVFPPR
180 RFKTVHDVAH FAARLLDGIL SHREMLDSGE LPLERAASRE KNQPLCMAQY YRLLGSCRRP
240 GVKQDSQFLP SRERLNDEDR HVVVICRNQM YCVVLQASDR GKLSESEIAS QILYVLSDAP
300 CLPAKPVPVG LLTAEPRSTW ARDREMLQED ERNQRNLELI ETAQVVLCLD EPLAGNFNAR
360 GFTGATPTVH RAGDRDETNM AHEMIHGGGS EYNSGNRWFD KTMQLIICTD GTWGLCYEHS
420 CSEGIAVVQL LEKIYKKIEE HPDEDNGLPQ HHLPPPERLE WHVGPQLQLR FAQASKSVDK
480 CIDDLDFYVY RYQSYGKTFI KSCQVSPDVY IQLALQLAHY KLYGRLVATY ESASTRRFLH
540 GRVDCIRAAS TEALEWAKAM CQGEGANVPL ESDREDEEES RKVKFSIYSK DHLRELFRCA
600 VARQTEVMVK NILGNGIDIP LLGLREASIE VTGEMHELFK DESYIISQCF LLSTSQVACS
660 TDSFMGYGPV TPRGYGCSYN PHPEQIVFCV SAFYSCEDTS ASRYAKSLQD SLDIMRDLLQ
720 N
Download this sequence
in fasta format
Download all sequences for 2.3.1.6
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
402183
Itoh N.,Slemmon J.R.,Hawke D.H.,Williamson R.,Morita E.,Itakura K.,Roberts E.,Shively J.E.,Crawford G.D.,Salvaterra P.M.
Cloning of Drosophila choline acetyltransferase cDNA.
Proc. Natl. Acad. Sci. U.S.A.
83
4081-4085
1986
402184
Sugihara H.,Andrisani V.,Salvaterra P.M.
Drosophila choline acetyltransferase uses a non-AUG initiation codon and full length RNA is inefficiently translated.
J. Biol. Chem.
265
21714-21719
1990
402186
Sugihara H.,Andrisani V.,Salvaterra P.M.
Genomic organization of Drosophila choline acetyltransferase.
J. Neurochem.
57
1636-1642
1991
402187
Adams M.D.,Celniker S.E.,Holt R.A.,Evans C.A.,Gocayne J.D.,Amanatides P.G.,Scherer S.E.,Li P.W.,Hoskins R.A.,Galle R.F.,George R.A.,Lewis S.E.,Richards S.,Ashburner M.,Henderson S.N.,Sutton G.G.,Wortman J.R.,Yandell M.D.,Zhang Q.,Chen L.X.,Brandon R.C.,Rogers Y.-H.C.,Blazej R.G.,Champe M.,Pfeiffer B.D.,Wan K.H.,Doyle C.,Baxter E.G.,Helt G.,Nelson C.R.,Miklos G.L.G.,Abril J.F.,Agbayani A.,An H.-J.,Andrews-Pfannkoch C.,Baldwin D.,Ballew R.M.,Basu A.,Baxendale J.,Bayraktaroglu L.,Beasley E.M.,Beeson K.Y.,Benos P.V.,Berman B.P.,Bhandari D.,Bolshakov S.,Borkova D.,Botchan M.R.,Bouck J.,Brokstein P.,Brottier P.,Burtis K.C.,Busam D.A.,Butler H.,Cadieu E.,Center A.,Chandra I.,Cherry J.M.,Cawley S.,Dahlke C.,Davenport L.B.,Davies P.,de Pablos B.,Delcher A.,Deng Z.,Mays A.D.,Dew I.,Dietz S.M.,Dodson K.,Doup L.E.,Downes M.,Dugan-Rocha S.,Dunkov B.C.,Dunn P.,Durbin K.J.,Evangelista C.C.,Ferraz C.,Ferriera S.,Fleischmann W.,Fosler C.,Gabrielian A.E.,Garg N.S.,Gelbart W.M.,Glasser K.,Glodek A.,Gong F.,Gorrell J.H.,Gu Z.,Guan P.,Harris M.,Harris N.L.,Harvey D.A.,Heiman T.J.,Hernandez J.R.,Houck J.,Hostin D.,Houston K.A.,Howland T.J.,Wei M.-H.,Ibegwam C.,Jalali M.,Kalush F.,Karpen G.H.,Ke Z.,Kennison J.A.,Ketchum K.A.,Kimmel B.E.,Kodira C.D.,Kraft C.L.,Kravitz S.,Kulp D.,Lai Z.,Lasko P.,Lei Y.,Levitsky A.A.,Li J.H.,Li Z.,Liang Y.,Lin X.,Liu X.,Mattei B.,McIntosh T.C.,McLeod M.P.,McPherson D.,Merkulov G.,Milshina N.V.,Mobarry C.,Morris J.,Moshrefi A.,Mount S.M.,Moy M.,Murphy B.,Murphy L.,Muzny D.M.,Nelson D.L.,Nelson D.R.,Nelson K.A.,Nixon K.,Nusskern D.R.,Pacleb J.M.,Palazzolo M.,Pittman G.S.,Pan S.,Pollard J.,Puri V.,Reese M.G.,Reinert K.,Remington K.,Saunders R.D.C.,Scheeler F.,Shen H.,Shue B.C.,Siden-Kiamos I.,Simpson M.,Skupski M.P.,Smith T.J.,Spier E.,Spradling A.C.,Stapleton M.,Strong R.,Sun E.,Svirskas R.,Tector C.,Turner R.,Venter E.,Wang A.H.,Wang X.,Wang Z.-Y.,Wassarman D.A.,Weinstock G.M.,Weissenbach J.,Williams S.M.,Woodage T.,Worley K.C.,Wu D.,Yang S.,Yao Q.A.,Ye J.,Yeh R.-F.,Zaveri J.S.,Zhan M.,Zhang G.,Zhao Q.,Zheng L.,Zheng X.H.,Zhong F.N.,Zhong W.,Zhou X.,Zhu S.C.,Zhu X.,Smith H.O.,Gibbs R.A.,Myers E.W.,Rubin G.M.,Venter J.C.
The genome sequence of Drosophila melanogaster.
Science
287
2185-2195
2000
402188
Misra S.,Crosby M.A.,Mungall C.J.,Matthews B.B.,Campbell K.S.,Hradecky P.,Huang Y.,Kaminker J.S.,Millburn G.H.,Prochnik S.E.,Smith C.D.,Tupy J.L.,Whitfield E.J.,Bayraktaroglu L.,Berman B.P.,Bettencourt B.R.,Celniker S.E.,de Grey A.D.N.J.,Drysdale R.A.,Harris N.L.,Richter J.,Russo S.,Schroeder A.J.,Shu S.Q.,Stapleton M.,Yamada C.,Ashburner M.,Gelbart W.M.,Rubin G.M.,Lewis S.E.
Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.
Genome Biol.
3
0-0
2002
402189
Stapleton M.,Carlson J.W.,Brokstein P.,Yu C.,Champe M.,George R.A.,Guarin H.,Kronmiller B.,Pacleb J.M.,Park S.,Wan K.H.,Rubin G.M.,Celniker S.E.
A Drosophila full-length cDNA resource.
Genome Biol.
3
0-0
2002
402190
Slemmon J.R.
Sequence analysis of a proteolyzed site in Drosophila choline acetyltransferase.
J. Neurochem.
52
1898-1904
1989
402191
Slemmon J.R.,Campbell G.A.,Selski D.J.,Bramson H.N.
The amino terminus of the putative Drosophila choline acetyltransferase precursor is cleaved to yield the 67 kDa enzyme.
Brain Res. Mol. Brain Res.
9
245-252
1991
402193
Carbini L.A.,Hersh L.B.
Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis.
J. Neurochem.
61
247-253
1993