carbamate kinase [Escherichia coli].

LOCUS       WP_000038002             310 aa            linear   BCT 24-APR-2020
ACCESSION   WP_000038002
VERSION     WP_000038002.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia coli"
                     /db_xref="taxon:562"
     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=32982
     Region          1..310
                     /region_name="PRK12353"
                     /note="putative amino acid kinase; Reviewed"
                     /db_xref="CDD:237071"
     Site            order(8,10..11,47..49,127,209..211)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(11,230..231,236,239,264,268..269,272)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(11,230..231,236,239,264,268..269,272)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:239768"
     Site            order(57,72,75..76,79,83..84,87,90..91,95,108..110,112,
                     170,173,201,203)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:239768"
ORIGIN      
        1 mskkivlalg gnalgddlag qmkavkitsq aivdliaqgh evivthgngp qvgminqafe
       61 aaakteahsp mlpmsvcval sqgyigydlq nalreellsr ginkpvvtlv tqvevdandp
      121 aflnptkpig sffteqeaeq ltkqgytlke dagrgyrrvv aspkpvdiie ketvkalvea
      181 gqvvitvggg gipviregnh lrgasavidk dwasarlaem idadmliilt avekvainfg
      241 keneqwldrl slsdaerfie eghfakgsml pkveaaasfa rsragreali tvlskakegi
      301 egktgtvicq