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Sequence of ACLY_RAT

EC Number:2.3.3.8

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
ATP citrate synthase
P16638
Rattus norvegicus
1100
120636
Reaction
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Other sequences found for EC No. 2.3.3.8

General information:

Sequence
show sequence in fasta format
   0 MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL LSQSLVVKPD
  60 QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG FLKNFLIEPF VPHSQAEEFY
 120 VCIYATREGD YVLFHHEGGV DVGDVDTKAQ KLLVGVDEKL NAEDIKRHLL VHAPEDKKEI
 180 LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP
 240 PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE
 300 LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA
 360 IRDYQGSLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMAWA
 420 PAIPNQPPTA AHTANFLLNA SGSTSTPAPS RTASFSESRA DEVAPAKKAK PAMPQDSVPS
 480 PRSLQGKSAT LFSRHTKAIV WGMQTRAVQG MLDFDYVCSR DEPSVAAMVY PFTGDHKQKF
 540 YWGHKEILIP VFKNMADAMK KHPEVDVLIN FASLRSAYDS TMETMNYAQI RTIAIIAEGI
 600 PEALTRKLIK KADQKGVTII GPATVGGIKP GCFKIGNTGG MLDNILASKL YRPGSVAYVS
 660 RSGGMSNELN NIISRTTDGV YEGVAIGGDR YPGSTFMDHV LRYQDTPGVK MIVVLGEIGG
 720 TEEYKICRGI KEGRLTKPVV CWCIGTCATM FSSEVQFGHA GACANQASET AVAKNQALKE
 780 AGVFVPRSFD ELGEIIQSVY EDLVAKGAIV PAQEVPPPTV PMDYSWAREL GLIRKPASFM
 840 TSICDERGQE LIYAGMPITE VFKEEMGIGG VLGLLWFQRR LPKYSCQFIE MCLMVTADHG
 900 PAVSGAHNTI ICARAGKDLV SSLTSGLLTI GDRFGGALDA AAKMFSKAFD SGIIPMEFVN
 960 KMKKEGKLIM GIGHRVKSIN NPDMRVQILK DFVKQHFPAT PLLDYALEVE KITTSKKPNL
1020 ILNVDGFIGV AFVDMLRNCG SFTREEADEY VDIGALNGVF VLGRSMGFIG HYLDQKRLKQ
1080 GLYRHPWDDI SYVLPEHMSM
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
894627
Elshourbagy N.A.,Near J.C.,Kmetz P.J.,Sathe G.M.,Southan C.,Strickler J.E.,Gross M.,Young J.F.,Wells T.N.C.,Groot P.H.E.
Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ, and age.
J. Biol. Chem.
265
1430-1435
1990
894628
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
894629
Moon Y.-A.,Kim K.-S.,Park S.-W.,Kim Y.-S.
Cloning and identification of exon-intron organization of the rat ATP-citrate lyase gene.
Biochim. Biophys. Acta
1307
280-284
1996
894630
Ramakrishna S.,D'Angelo G.,Benjamin W.B.
Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3 like kinase).
Biochemistry
29
7617-7624
1990
894631
Lord K.A.,Wang X.M.,Simmons S.J.,Bruckner R.C.,Loscig J.,O'Connor B.,Bentley R.,Smallwood A.,Chadwick C.C.,Stevis P.E.,Ciccarelli R.B.
Variant cDNA sequences of human ATP:citrate lyase: cloning, expression, and purification from baculovirus-infected insect cells.
Protein Expr. Purif.
9
133-141
1997
894632
Berwick D.C.,Hers I.,Heesom K.J.,Moule S.K.,Tavare J.M.
The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes.
J. Biol. Chem.
277
33895-33900
2002
894633
Moser K.,White F.M.
Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.
J. Proteome Res.
5
98-104
2006
894634
Lundby A.,Secher A.,Lage K.,Nordsborg N.B.,Dmytriyev A.,Lundby C.,Olsen J.V.
Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
Nat. Commun.
3
876-876
2012