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LOCUS WP_003100033 310 aa linear BCT 20-NOV-2023 ACCESSION WP_003100033 VERSION WP_003100033.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. 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="Pseudomonas" /db_xref="taxon:286" 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=32949 Region 1..309 /region_name="PRK12354" /note="carbamate kinase; Reviewed" /db_xref="CDD:183466" Site order(6,8..9,49..51,122,206..208) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:239768" Site order(9,227..228,233,236,257,261..262,265) /site_type="other" /note="nucleotide binding site [chemical binding]" /db_xref="CDD:239768" Site order(9,227..228,233,236,257,261..262,265) /site_type="other" /note="nucleotide binding site [chemical binding]" /db_xref="CDD:239768" Site order(59,70,73..74,77,81..82,85,88..89,93,103..105,107, 165,168,198,200) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:239768" ORIGIN 1 mrivvalggn allrrgepmt adnqrenvri aaeqiakvap gnelviahgn gpqvgllalq 61 gaaydkvspy pldvlgaete gmigymieqe mgnllpfevp fatiltqvev dgkdpafqnp 121 tkpigpvysr eeaerlaaek gwsiapdgdk frrvvpsprp krifeirpvk wllekgtivi 181 caggggiptm ydeagkklsg veavidkdlc ssllaqelva diliiatdvd aayvdwgkpt 241 qkaiaqahpd elerlgfaag smgpkvqaai efaratgkda vigsladiva itegkagtrv 301 strkagieyr