MULTISPECIES: pyruvate dehydrogenase (acetyl-transferring),

LOCUS       WP_000003820             887 aa            linear   BCT 07-MAY-2024
            homodimeric type [Bacteria].
ACCESSION   WP_000003820
VERSION     WP_000003820.1
KEYWORDS    RefSeq.
SOURCE      Bacteria (eubacteria)
  ORGANISM  Bacteria
            Unclassified.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Inoue,H., Inagaki,K., Eriguchi,S.I., Tamura,T., Esaki,N., Soda,K.
            and Tanaka,H.
  TITLE     Molecular characterization of the mde operon involved in
            L-methionine catabolism of Pseudomonas putida
  JOURNAL   J Bacteriol 179 (12), 3956-3962 (1997)
   PUBMED   9190812
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 :: TIGR00759.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Bacteria"
                     /db_xref="taxon:2"
     gene            1..887
                     /gene="aceE"
     Protein         1..887
                     /product="pyruvate dehydrogenase (acetyl-transferring),
                     homodimeric type"
                     /EC_number="1.2.4.1"
                     /GO_component="GO:0045254 - pyruvate dehydrogenase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004738 - pyruvate dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006086 - acetyl-CoA biosynthetic process
                     from pyruvate [Evidence IEA]"
                     /calculated_mol_wt=99538
     Region          1..887
                     /region_name="aceE"
                     /note="pyruvate dehydrogenase subunit E1; Reviewed;
                     PRK09405"
                     /db_xref="CDD:236500"
ORIGIN      
        1 mserfpndvd pietrdwlqa iesvireegv eraqylidql laearkggvn vaagtgisny
       61 intipveeqp eypgnleler rirsairwna imtvlraskk dlelgghmas fqssatiydv
      121 cfnhffrarn eqdggdlvyf qghispgvya raflegrltq eqldnfrqev hgnglssyph
      181 pklmpefwqf ptvsmglgpi gaiyqakflk ylehrglkdt skqtvyaflg dgemdepesk
      241 gaitiatrek ldnlvfvinc nlqrldgpvt gngkiinele gifegagwnv ikvmwgsrwd
      301 ellrkdtsgk liqlmnetvd gdyqtfkskd gayvrehffg kypetaalva dwtdeqiwal
      361 nrgghdpkki yaafkkaqet kgkatvilah tikgygmgda aegkniahqv kkmnmdgvrh
      421 irdrfnvpvs dadieklpyi tfpegseeht ylhaqrqklh gylpsrqpnf teklelpslq
      481 dfgalleeqs keisttiafv ralnvmlknk sikdrlvpii adeartfgme glfrqigiys
      541 pngqqytpqd reqvayyked ekgqilqegi nelgagcswl aaatsystnn lpmipfyiyy
      601 smfgfqrigd lcwaagdqqa rgfliggtsg rttlngeglq hedghshiqs ltipncisyd
      661 payayevavi mhdglermyg ekqenvyyyi ttlnenyhmp ampegaeegi rkgiykleti
      721 egskgkvqll gsgsilrhvr eaaeilakdy gvgsdvysvt sftelardgq dcerwnmlhp
      781 letprvpyia qvmndapava stdymklfae qvrtyvpadd yrvlgtdgfg rsdsrenlrh
      841 hfevdasyvv vaalgelakr geidkkvvad aiakfnidad kvnprla