Reviewed, UniProtKB/Swiss-Prot Q54M22 (ODBA_DICDI)

Names and origin

Protein names

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

Gene names

Name:	bkdA
ORF Names:	DDB_G0286335

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	441 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.
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Heterotetramer of alpha and beta chains By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Miscellaneous	Bound potassium ions stabilize the protein structure By similarity.
Sequence similarities	Belongs to the BCKDHA family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Potassium Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 17	17	Mitochondrion Potential
	Chain	18 – 441	424	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial		PRO_0000327985
Regions
	Region	145 – 147	3	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	194	1	Potassium By similarity
	Metal binding	199	1	Potassium By similarity
	Metal binding	200	1	Potassium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54M22-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: E4ECC73ADFFC0538	FASTA	441	50,326
	10 20 30 40 50 60 MISQSYRILS RISRNNELKK TFLTNLNCKS SSPSIIRSFC KKQNLDENFE YTNKLEVQEL 70 80 90 100 110 120 KHYIPCYTIM DQEGVVSKPD QDPNFSKEEV IKMYTTMLTL NVMDSILYDV QRQGRISFYM 130 140 150 160 170 180 TSFGEEAIHI GSAAALEMSD TIFAQYRETG VFMWRGFTIN DIINQCCTNE HDLGKGRQMP 190 200 210 220 230 240 MHFGSRKINL QTISSPLTTQ LPQAVGSSYA QKLAGEKNCT IVYFGEGAAS EGDFHAAMNF 250 260 270 280 290 300 AAALSTPTIF FCRNNKWAIS TPSKEQYKGD GIAGRGPNGY GMKTIRVDGN DIWAVYNVTK 310 320 330 340 350 360 LARKIAVEEQ VPVLIEAMTY RVGHHSTSDD SSRYRTVEEI NAWKEGKNPI SRLRNYMNHK 370 380 390 400 410 420 GWWSDAQEKE TIANARTTVR ESLVNAEKQY KPSINEIFTD VYDKPTPNLI EQQKELIEHL 430 440 KLYPDEYPLN QFADSKLILK D

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
EMBLGenBankDDBJ	AAFI02000085 Genomic DNA. Translation: EAL64343.1.
RefSeq	XP_637809.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3389368.
KEGG	ddi:DDB_0230190.
Organism-specific databases
dictyBase	DDB_G0286335. bkdA.
Phylogenomic databases
OMA	Q54M22. MENFMNQ.
Enzyme and pathway databases
BRENDA	1.2.4.4. 424.
Family and domain databases
InterPro	IPR001017. DH_E1. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODBA_DICDI

Accession

Primary (citable) accession number: Q54M22

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)