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  • This record is a non-redundant protein sequence. Please read more here.

MULTISPECIES: pyruvate dehydrogenase (acetyl-transferring), homodimeric type [Pseudoalteromonas]

NCBI Reference Sequence: WP_024600130.1

Identical Proteins FASTA Graphics 

LOCUS       WP_024600130             888 aa            linear   BCT 07-MAY-2024
DEFINITION  MULTISPECIES: pyruvate dehydrogenase (acetyl-transferring),
            homodimeric type [Pseudoalteromonas].
ACCESSION   WP_024600130
VERSION     WP_024600130.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 888)
  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..888
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     gene            1..888
                     /gene="aceE"
     Protein         1..888
                     /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=99406
     Region          1..888
                     /region_name="aceE"
                     /note="pyruvate dehydrogenase subunit E1; Reviewed;
                     PRK09405"
                     /db_xref="CDD:236500"
ORIGIN      
        1 msevnkidvd aletqewlqa lesvvreegv eraqflleqv leqarldgvd mptgittnyv
       61 ntipvdqepa ypgdvnlerr irsiirwnai mivlraskkd ldlgghmasy qssaafyevc
      121 fnhffkapnd vdggdlvyyq ghispgiyar afvegrlsaa qldnfrqevd geglpsyphp
      181 klmpefwqfp tvsmglgpis siyqarflky ldgrglkdtk nqrvyaflgd gemdepesrg
      241 aisfaarekl dnlcylvncn lqrldgpvmg ngkiiqeleg lfkgagwnvi klvwgsgwdi
      301 llakdttgkl lqlmnetvdg dyqtykakdg ayvrenffgr ypetaalvad mtddeifalk
      361 rgghessklf aafkkaedtk grptvilakt vkgygmgeaa egkniahqvk kmdmshvahl
      421 rsrlglddlv seeqlkelpy leleegspey kylharrdel kgytpkripr fseklalpev
      481 eafkplleeq krdisttmgf vralnillkd kgigknivpi iadeartfgm eglfrqigiy
      541 nphgqnytpq drdivsyyke tvsgqvlqeg inelgamssw vaaatsystn dlpmipfyiy
      601 ysmfgfqrvg dmawmagdqq argfllgata grttlngegl qhedghshil antvpncisy
      661 dptyafevav ivqdgirrmy gddqeniyyy ltlmnenyhq pampegaeeg irkgiykles
      721 yegkkanvql lssgtimtev rkaaailsee ygiasdvfsv tsfneltreg qdverfnmln
      781 pegeqktafi tsvlndsvtv aatdymknya eqarsfipss nykvlgtdgy grsdsrenlr
      841 rhfevnagyv vvatlselak rgeveksvvv ealkkfnidt nklnplya
//
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