GenomeNet

Database: RefSeq
Entry: WP_012405686
LinkDB: WP_012405686
Original site: WP_012405686 
LOCUS       WP_012405686             501 aa            linear   BCT 23-APR-2018
DEFINITION  form I ribulose bisphosphate carboxylase large subunit
            [Paraburkholderia phymatum].
ACCESSION   WP_012405686
VERSION     WP_012405686.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phymatum
  ORGANISM  Paraburkholderia phymatum
            Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
            Burkholderiaceae; Paraburkholderia.
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.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Paraburkholderia phymatum"
                     /db_xref="taxon:148447"
     Protein         1..501
                     /product="form I ribulose bisphosphate carboxylase large
                     subunit"
                     /EC_number="4.1.1.39"
                     /calculated_mol_wt=55045
     Region          23..492
                     /region_name="rbcL"
                     /note="ribulose bisophosphate carboxylase; Reviewed;
                     PRK04208"
                     /db_xref="CDD:179787"
     Region          38..490
                     /region_name="RuBisCO_large_I"
                     /note="Ribulose bisphosphate carboxylase large chain, Form
                     I; cd08212"
                     /db_xref="CDD:173977"
     Site            order(60,75,77..78,80..87,90,95,124..128,130,132..133,
                     136..137,139..141,143..146,148..150,193..197,222..223,
                     225..229,231,261..266,271,286,289..293,295..296,311,
                     313..314,316..318,320..321,324..326,348..353,398..400,
                     421..422,424..427,429..430,479,482,484,486..487,489)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:173977"
     Site            order(75,80..81,141,191,193,195,221..222,311..312,344,
                     351..352,396..398,420..421)
                     /site_type="active"
                     /db_xref="CDD:173977"
     Site            order(174,179,181..185,212..214,244,247..253,276,281,306,
                     414,427..428,432,435,438..439,442..443,446,448..450,468,
                     470)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:173977"
     Site            219
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:173977"
     Site            221..222
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:173977"
ORIGIN      
        1 mndfskeavk padsataaak aekrsryaag vmkyremgyw qpdytpkdtd vialfritpq
       61 pgvepeeaaa avagesstat wtvvwtdrlt acdmyrakaf rvepvpnpae gepqyfafia
      121 yeldlfeegs vanltasiig nvfgfkplka lrledmripv aylktfqgpp tgivvererl
      181 dkygrpllga tvkpklglsg knygrvvyeg lkggldflkd deninsqpfm hwrdrylfam
      241 eavhraqaet gevkghylnv tagtmedmye raefakelgs civmidlvig wtaitsmgrw
      301 arkndmilhl hraghgtytr qrnhgisfrv iakwlrmagv dhahagtavg kldgdplsvq
      361 gyynvlresh nsvdltrgif fdqhwaglrk vmpvasggih agqmhqlldl fgddailqfg
      421 ggtighpsgi qagatanrva letmvkarne grdianegsd lleaaarhct plkqaldtwg
      481 dvtfnytptd spdfavtpsv a
//
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