Sequence of Q75VW8_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
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>Q75VW8|citrate-CoA ligase|EC 6.2.1.18|Hydrogenobacter thermophilus|TrEMBL
MNLYEYEAYDKIFKKYGIPTPEYMFESSVSDRLVEFVNQLGECVVKSQVLVGKRGKAGAV
KVCSDPQSAIETAQALLNYPVYGEMPVGVLVARKVNILKELYASITYSTEVRAPVLTLSL
EGGMDIEEVPPEKVRSWTINPLKGLYPHMVRNYLLELGFPQEYMGILRELSEVVSNMYRA
FWEAEARLLEINPLAICDVNGKLKVYALDAVVTIDDDASVPPSKIYGVRTAMKRPPTERE
IEASLIDRDDHRGKAGSYVEVDGDIAMMTFGGGGSTVTIETTYAIGLKPANFTDIGGNPP
AEKMYKITKIILSKPGIRGVLVCGGTANNTRIDVTLGEGVANAIRDLYKEGKLNPDWIWV
VRRNGPEAEKGLRMLYEAFKECKVKGEIYDSSLPLTEAPIRLKELLDICTSAQSEDRHLT
EEQAKDMGI
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
131263066
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
131263067
Aoshima M.
Novel enzyme reactions related to the tricarboxylic acid cycle: phylogenetic/functional implications and biotechnological applications.
Appl. Microbiol. Biotechnol.
75
249-255
2007
131263068
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
