MULTISPECIES: pyruvate dehydrogenase (acetyl-transferring) E1

LOCUS       WP_003722679             371 aa            linear   BCT 07-MAY-2024
            component subunit alpha [Listeria].
ACCESSION   WP_003722679
VERSION     WP_003722679.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
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 :: TIGR03181.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     gene            1..371
                     /gene="pdhA"
     Protein         1..371
                     /product="pyruvate dehydrogenase (acetyl-transferring) E1
                     component subunit alpha"
                     /GO_component="GO:0045254 - pyruvate dehydrogenase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004739 - pyruvate dehydrogenase
                     (acetyl-transferring) activity [Evidence IEA]"
                     /GO_process="GO:0006086 - acetyl-CoA biosynthetic process
                     from pyruvate [Evidence IEA]"
                     /calculated_mol_wt=41136
     Region          24..365
                     /region_name="PDH_E1_alph_x"
                     /note="pyruvate dehydrogenase E1 component, alpha subunit;
                     TIGR03181"
                     /db_xref="CDD:213783"
     Site            order(105..106,145,147,175..178,205,207,274)
                     /site_type="other"
                     /note="TPP-binding site [chemical binding]"
                     /db_xref="CDD:238958"
     Site            order(127,145..146,177,179..182,185,189,193,208..211,225,
                     230,279,283)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            order(140,142,144,149,152..153,156..157,159..160,163,
                     182..183,189..190,193)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            order(269..275,277,279..288,296..298)
                     /site_type="phosphorylation"
                     /note="phosphorylation loop region [posttranslational
                     modification]"
                     /db_xref="CDD:238958"
ORIGIN      
        1 masktkkaii dvkkqfeavh kqfelvqiln ekgeivnpdl mpdltddqlv elmtrmvwtr
       61 vldqrsisln rqgrlgfyap tagqeasqla shyalekhdy ilpgyrdvpq liwhglpltk
      121 aflfsrghfv gnqfpedlnv lspqiiigaq ivqaagvalg lkkrkkdavv itytgdggss
      181 qgdfyegmnf agayhapaif vvqnnkfais tprekqsaae tlaqkavaag ipgvqvdgmd
      241 plavyavtkf areravageg ptlietmtyr ygphtlsgdd ptryrtkeld gewelkdpiv
      301 rfrtflegkg lwneekenav idqakeeikv aikeadatpk qtvtdllknm yetptapike
      361 qlaiyeakes k