Reviewed, UniProtKB/Swiss-Prot Q55FN7 (ODBB_DICDI)

Names and origin

Protein names

Recommended name:
    2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
    EC=1.2.4.4
Alternative name(s):
    Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
      Short name=BCKDH E1-beta
      Short name=BCKDE1B
    3-methyl-2-oxobutanoate dehydrogenase

Gene names

Name:	bkdB
ORF Names:	DDB_G0268020

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.
Subunit structure	Heterodimer of an alpha and a beta chain By similarity.
Subcellular location	Mitochondrion matrix By similarity.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial alpha-ketoglutarate dehydrogenase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion Potential
	Chain	26 – 370	345	2-oxoisovalerate dehydrogenase subunit beta, mitochondrial		PRO_0000327589

Sequences

	Sequence		Length	Mass (Da)
	Q55FN7-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 083E690721B9559D	FASTA	370	40,725
	10 20 30 40 50 60 MLRGNNIKKV NSLLVRSFHS TVGNRSGGPS TPINYPSLEI ENAGEKQKMN LFQAINNGMD 70 80 90 100 110 120 IAMQKDSKAV VFGEDVGFGG VFRCTVGLRD KYGASRVFNT PLCEQGIAGF AIGLAAQGAT 130 140 150 160 170 180 PIAEIQFADY IFPAFDQIVN EAAKYRYRSG GQFDCGSLTI RSPYGAVGHG GHYHSQSPES 190 200 210 220 230 240 YFGHTPGLKV VIPSTPIEAK GLLLASIREK DPVIFFEPKL MYRSAVEEVP IGDYEIPLGK 250 260 270 280 290 300 ARIVKEGKDI TIIGWGAQMR VLLQAVNMAE EKLGISCELI DLRTIQPWDV ETVVESVKKT 310 320 330 340 350 360 GRVVISHEAP KTGGWAAEIS ATIQERCFLH LEAPIQRVCG YDTPFPLIFE KFYVPDHLKN 370 FESIKKTMVY

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000003 Genomic DNA. Translation: EAL73463.1.
RefSeq	XP_647496.1.
3D structure databases
HSSP	HSSP built from PDB template 2BFF based on UniProtKB P21953.
SMR	Q55FN7. Positions 44-370.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55FN7.
Genome annotation databases
GeneID	8616303.
KEGG	ddi:DDB_0230185.
Organism-specific databases
dictyBase	DDB_G0268020. bkdB.
Phylogenomic databases
eggNOG	KOG0525.
HOGENOM	HBG753264.
OMA	ASIRRTG.
PhylomeDB	Q55FN7.
Enzyme and pathway databases
BRENDA	1.2.4.4. 424.
Family and domain databases
InterPro	IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODBB_DICDI

Accession

Primary (citable) accession number: Q55FN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)