Sequence of CPKA_PYRFU
EC Number:2.7.2.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
carbamate kinase
P95474
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
314
34429
Reaction
ATP + carbamate = ADP + carbamoyl phosphate
Other sequences found for EC No. 2.7.2.2
General information:
Sequence
0 MGKRVVIALG GNALQQRGQK GSYEEMMDNV RKTARQIAEI IARGYEVVIT HGNGPQVGSL
60 LLHMDAGQAT YGIPAQPMDV AGAMSQGWIG YMIQQALKNE LRKRGMEKKV VTIITQTIVD
120 KNDPAFQNPT KPVGPFYDEE TAKRLAREKG WIVKEDSGRG WRRVVPSPDP KGHVEAETIK
180 KLVERGVIVI ASGGGGVPVI LEDGEIKGVE AVIDKDLAGE KLAEEVNADI FMILTDVNGA
240 ALYYGTEKEQ WLREVKVEEL RKYYEEGHFK AGSMGPKVLA AIRFIEWGGE RAIIAHLEKA
300 VEALEGKTGT QVLP
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
913569
Durbecq V.,Legrain C.,Roovers M.,Pierard A.,Glansdorff N.
The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus, a missing link in the evolution of carbamoyl phosphate biosynthesis.
Proc. Natl. Acad. Sci. U.S.A.
94
12803-12808
1997
913571
Maeder D.L.,Weiss R.B.,Dunn D.M.,Cherry J.L.,Gonzalez J.M.,DiRuggiero J.,Robb F.T.
Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences.
Genetics
152
1299-1305
1999
913572
Ramon-Maiques S.,Marina A.,Uriarte M.,Fita I.,Rubio V.
The 1.5-A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases.
J. Mol. Biol.
299
463-476
2000
