Sequence of Q75VW6_HYDTH
EC Number:6.2.1.18
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA
Other sequences found for EC No. 6.2.1.18
General information:
Sequence
0 MERRWKIGTP YLNDSTRIIV MGITGREASQ VVAESEALYP GFVVAGVTPG KGGSEVAGVP
60 VYNTVREAQE RHPEINTGIV YVPPASVKDA VIELIDAGIG VIFIITEHVP IRDTVYFYHY
120 AKERGTIIVG PTSLGCIIPK IPARIGAIGG KDPSVAYADG GLVILSKSGG LTTTTAEMFK
180 RRGWGVYMAL ALGGDVISCT TFADAIENLA DDPNVKGVII QGEVGGSYEE QAAETILRLW
240 KEGRWNKPVA AFVAGRFQES LEGVSFGHAG AIVERGKGKA TDKIRAFNEV GKITGLVKVA
300 EFYHDLVHCI EELGVPRDFE DSTPEGKVKP LYSTINEENC QFKA
Download this sequence
in fasta formatDownload all sequences for 6.2.1.18
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
178589674
Aoshima M.,Ishii M.,Igarashi Y.
A novel enzyme, citryl-CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6.
Mol. Microbiol.
52
751-761
2004
178589675
Aoshima M.
Novel enzyme reactions related to the tricarboxylic acid cycle: phylogenetic/functional implications and biotechnological applications.
Appl. Microbiol. Biotechnol.
75
249-255
2007
178589676
Verschueren K.,Blanchet C.,Felix J.,Dansercoer A.,De Vos D.,Bloch Y.,Van Beeumen J.,Svergun D.,Gutsche I.,Savvides S.N.,Verstraete K.
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.
Nature
568
571-575
2019
