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LOCUS WP_000428751 310 aa linear BCT 24-APR-2020 ACCESSION WP_000428751 VERSION WP_000428751.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 310) AUTHORS Ramon-Maiques,S., Marina,A., Guinot,A., Gil-Ortiz,F., Uriarte,M., Fita,I. and Rubio,V. TITLE Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria JOURNAL J. Mol. Biol. 397 (5), 1261-1275 (2010) PUBMED 20188742 REFERENCE 2 (residues 1 to 310) AUTHORS Uriarte,M., Marina,A., Ramon-Maiques,S., Fita,I. and Rubio,V. TITLE The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase JOURNAL J. Biol. Chem. 274 (23), 16295-16303 (1999) PUBMED 10347186 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR00746.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..310 /organism="Salmonella" /db_xref="taxon:590" gene 1..310 /gene="arcC" Protein 1..310 /product="carbamate kinase" /EC_number="2.7.2.2" /GO_function="GO:0008804 - carbamate kinase activity [Evidence IEA]" /GO_process="GO:0006520 - cellular amino acid metabolic process [Evidence IEA]" /calculated_mol_wt=33219 Region 6..310 /region_name="PRK12354" /note="carbamate kinase; Reviewed" /db_xref="CDD:183466" Site order(10,12..13,53..55,125,207..209) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:239768" Site order(13,228..229,234,237,258,262..263,266) /site_type="other" /note="nucleotide binding site [chemical binding]" /db_xref="CDD:239768" Site order(13,228..229,234,237,258,262..263,266) /site_type="other" /note="nucleotide binding site [chemical binding]" /db_xref="CDD:239768" Site order(63,74,77..78,81,85..86,89,92..93,97,107..108,110, 168,171,199,201) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:239768" ORIGIN 1 menkrtlvva lggnallkrg epleadiqrk nielaartia qltrqwrvvl vhgngpqvgl 61 lalqnsayan vtpypldilg aesqgmigym lqqalknhlp ereisvlltq vevdandpaf 121 lnptkyigpi ydeaqaralq aekgwvfkad gnafrrvvps pqpkrivend airalisrdh 181 lvicnggggv pvvekadgyh gieavidkdl saallasqih adalliltda davyldwgkp 241 tqrplaqvtp ellremqfda gsmgpkvtac aefvshcrgi agigsladgq ailagekgtl 301 ircetadvda