alpha-ketoacid dehydrogenase subunit beta [Shewanella oneidensis].
LOCUS WP_011072331 325 aa linear BCT 21-JUL-2024
ACCESSION WP_011072331
VERSION WP_011072331.1
KEYWORDS RefSeq.
SOURCE Shewanella oneidensis
ORGANISM Shewanella oneidensis
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
Alteromonadales; Shewanellaceae; Shewanella.
REFERENCE 1 (residues 1 to 325)
AUTHORS Costelloe,S.J., Ward,J.M. and Dalby,P.A.
TITLE Evolutionary analysis of the TPP-dependent enzyme family
JOURNAL J Mol Evol 66 (1), 36-49 (2008)
PUBMED 18043855
REFERENCE 2 (residues 1 to 325)
AUTHORS Aevarsson,A., Seger,K., Turley,S., Sokatch,J.R. and Hol,W.G.
TITLE Crystal structure of 2-oxoisovalerate and dehydrogenase and the
architecture of 2-oxo acid dehydrogenase multienzyme complexes
JOURNAL Nat Struct Biol 6 (8), 785-792 (1999)
PUBMED 10426958
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 :: Conserved Domain (CDD)
Evidence Accession :: Domain architecture ID 11414334
Evidence Source :: NCBI SPARCLE
##Evidence-For-Name-Assignment-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..325
/organism="Shewanella oneidensis"
/db_xref="taxon:70863"
Protein 1..325
/product="alpha-ketoacid dehydrogenase subunit beta"
/EC_number="1.2.4.-"
/GO_function="GO:0016491 - oxidoreductase activity
[Evidence IEA]"
/calculated_mol_wt=35241
Region 1..325
/region_name="AcoB"
/note="Pyruvate/2-oxoglutarate/acetoin dehydrogenase
complex, dehydrogenase (E1) component, beta subunit
[Energy production and conversion]; COG0022"
/db_xref="CDD:439793"
ORIGIN
1 maemnmlqav nealsiamqa dermvvfged vghfggvfra tsglqekfgr arcfntplte
61 qgiagfangl asngmtavae iqfadyifpa fdqivnesak fryrsgnefn vgslvfrtpy
121 gggiagghyh sqspeayftq tpglkvvvpr npaqakglll asirdknpvv ffepkrlyra
181 svgdvpagdy eielgkaevl regkditlva wgaqmeiiek aadmaakegi sceiidlrtl
241 apwdvntvad svkktgrllv nheapltggf ageiaatiqq ecflylespi srvcgldtpy
301 plvhekeymp dalktfeaik asvnf