MULTISPECIES: carbamate kinase [Vibrio].

LOCUS       WP_017053214             304 aa            linear   BCT 05-OCT-2022
ACCESSION   WP_017053214
VERSION     WP_017053214.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 304)
  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 304)
  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..304
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     gene            1..304
                     /gene="arcC"
     Protein         1..304
                     /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=32697
     Region          5..300
                     /region_name="PRK12354"
                     /note="carbamate kinase; Reviewed"
                     /db_xref="CDD:183466"
     Site            order(9,11..12,52..54,124,206..208)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(12,227..228,233,236,257,261..262,265)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(12,227..228,233,236,257,261..262,265)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(62,73,76..77,80,84..85,88,91..92,96,105..107,109,
                     167,170,198,200)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:239768"
ORIGIN      
        1 mtkqtvvval ggnallrrgq pleadiqren ietavktisk iaeeynvvlv hgngpqvgll
       61 alqgleykkv spypldvlga etqgmigyml mqefrnylpq thiscmltqm tvdpkdpafa
      121 dptkpigpiy eeaeakelae kyrwsikpdg khfrrvvpsp qptgiiesda ittlidqghl
      181 victggggip vkeengklvg veavidkdms aaflakqlda dalliltdad avyldwgkpt
      241 qhalsattps elsqyefdag smgpkieasc efikqggklv gigaledglr ilkgeagtni
      301 krda