carbamate kinase [Listeria monocytogenes].

LOCUS       WP_003721662             313 aa            linear   BCT 24-APR-2020
ACCESSION   WP_003721662
VERSION     WP_003721662.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 313)
  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 313)
  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..313
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     gene            1..313
                     /gene="arcC"
     Protein         1..313
                     /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=33364
     Region          1..312
                     /region_name="PRK12353"
                     /note="putative amino acid kinase; Reviewed"
                     /db_xref="CDD:237071"
     Site            order(8,10..11,50..52,128,211..213)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(11,232..233,238,241,266,270..271,274)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(11,232..233,238,241,266,270..271,274)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(60,73,76..77,80,84..85,88,91..92,96,109..111,113,
                     172,175,203,205)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:239768"
ORIGIN      
        1 mnqkivvalg gnailssdas aeaqrsalee taeylvqfie ngddliishg ngpqvgnlml
       61 qqhagasekn pampldtcva mtqgsigywm qnaldkaflk hgldkvavsl itqvvvdkdd
      121 pafekptkpi gpflnkeeae kemaetgaif ledagrgyrk vvpsprplsi kehqiikqlv
      181 dsgvvtisag gggvsvveng ldlsgvetvi dkdfasekla elidadllvi ltgvenvyin
      241 ynqpnqkkle qvtvseleky idekqfaags mlpkieaata fvkerphaka iitsleniga
      301 mlergagtvi vag