LOCUS       WP_010997950            1104 aa            linear   BCT 11-DEC-2019
DEFINITION  MULTISPECIES: carbamoyl-phosphate synthase large subunit
            [Nostocaceae].
ACCESSION   WP_010997950
VERSION     WP_010997950.1
KEYWORDS    RefSeq.
SOURCE      Nostocaceae
  ORGANISM  Nostocaceae
            Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Thoden,J.B., Huang,X., Kim,J., Raushel,F.M. and Holden,H.M.
  TITLE     Long-range allosteric transitions in carbamoyl phosphate synthetase
  JOURNAL   Protein Sci. 13 (9), 2398-2405 (2004)
   PUBMED   15322282
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Miles,B.W., Thoden,J.B., Holden,H.M. and Raushel,F.M.
  TITLE     Inactivation of the amidotransferase activity of carbamoyl
            phosphate synthetase by the antibiotic acivicin
  JOURNAL   J. Biol. Chem. 277 (6), 4368-4373 (2002)
   PUBMED   11729189
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Thoden,J.B., Raushel,F.M., Benning,M.M., Rayment,I. and Holden,H.M.
  TITLE     The structure of carbamoyl phosphate synthetase determined to 2.1 A
            resolution
  JOURNAL   Acta Crystallogr. D Biol. Crystallogr. 55 (Pt 1), 8-24 (1999)
   PUBMED   10089390
REFERENCE   4  (residues 1 to 1104)
  AUTHORS   Thoden,J.B., Holden,H.M., Wesenberg,G., Raushel,F.M. and Rayment,I.
  TITLE     Structure of carbamoyl phosphate synthetase: a journey of 96 A from
            substrate to product
  JOURNAL   Biochemistry 36 (21), 6305-6316 (1997)
   PUBMED   9174345
REFERENCE   5  (residues 1 to 1104)
  AUTHORS   Trotta,P.P., Pinkus,L.M., Haschemeyer,R.H. and Meister,A.
  TITLE     Reversible dissociation of the monomer of glutamine-dependent
            carbamyl phosphate synthetase into catalytically active heavy and
            light subunits
  JOURNAL   J. Biol. Chem. 249 (2), 492-499 (1974)
   PUBMED   4358555
REFERENCE   6  (residues 1 to 1104)
  AUTHORS   Khedouri,E., Anderson,P.M. and Meister,A.
  TITLE     Selective inactivation of the glutamine binding site of Escherichia
            coli carbamyl phosphate synthetase by
            2-amino-4-oxo-5-chloropentanoic acid
  JOURNAL   Biochemistry 5 (11), 3552-3557 (1966)
   PUBMED   5339592
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 :: NF003671.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05294
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Nostocaceae"
                     /db_xref="taxon:1162"
     gene            1..1104
                     /gene="carB"
     Protein         1..1104
                     /product="carbamoyl-phosphate synthase large subunit"
                     /EC_number="6.3.5.5"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006807 - nitrogen compound metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=121026
     Region          1..1100
                     /region_name="carB"
                     /note="carbamoyl-phosphate synthase large subunit;
                     PRK05294"
                     /db_xref="CDD:235393"
ORIGIN      
        1 mprrqdiqki lllgsgpivi gqacefdysg tqackalree gyevvlvnsn patimtdpet
       61 adrtyieplt pelvekviar erpdallptm ggqtalniav alakngvldq ynveligakl
      121 paiekaedrk lfneamdkig vkvcpsgtas sldeskaiar rigtypliir paftmggtgg
      181 giaynqeefe emaqvgidas pvsqilidqs llgwkeyele vmrdladnvv iicsienidp
      241 mgihtgdsit vapaqtltdk eyqrlrdmai kiireigvet ggsniqfavn pvngdvvvie
      301 mnprvsrssa lsskatgfpi akmaaklavg ytldeirndi tkktpasfep tidyvvtkvp
      361 rfafekfpgs epvlttqmks vgeamaigrt fnesfqkalr sletgragwg cdkaeklpsg
      421 eqiraqlrtp npdrifavrh alqlgmspee iyeltaidpw fldkmqqlle vekflkrtpl
      481 kqltreqmya vkrdgysdrq iafatktted evrayrkelg vtpvyktvdt caaefeaftp
      541 yyystyeeet evipaskpkv milgggpnri gqgiefdycc chaayalkga gyetimvnsn
      601 petvstdydt sdrlyfeplt kedvlniiea enpvgiivqf ggqtplklal plqdylrqvg
      661 ngslvigngn eetaitddql pitkiwgtsp dsidsaedre rfekilqkln isqppngiar
      721 syedalivak rigypvvvrp syvlggrame ivysdteler ymtfavqvep ehpilidkfl
      781 enaievdvda iadhtgrvvi ggimehieqa gihsgdsacs lpsislppav lnqirtwtvq
      841 laqelsvvgl mniqfaviga ssyspqvyil eanprasrtv pfvskatgvp laklaslims
      901 gktleelnft qevipshiav keavlpfnkf pgtdtilgpe mrstgevmgi dsdfgrafak
      961 aelgagerlp ltgtvfvsms drdksaavpv vrefidlgfk vmatfgtrrv llenglnvel
     1021 vlklhegrph vidaiknqki qliintpsge eaqtdarlir rtglaykipi ittiagakat
     1081 vaairsmqnt tldvktiqey cpnf
//