Reviewed, UniProtKB/Swiss-Prot P37940 (ODBA_BACSU)

Names and origin

Protein names

Recommended name:
    2-oxoisovalerate dehydrogenase subunit alpha
    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:	bfmBAA
Synonyms:	bfmB1a
Ordered Locus Names:	BSU24050

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activity	3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2).
Cofactor	Thiamine pyrophosphate.
Subunit structure	Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex.
Sequence similarities	Belongs to the BCKDHA family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC magnesium 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
	Chain	1 – 330	330	2-oxoisovalerate dehydrogenase subunit alpha		PRO_0000162248
Regions
	Region	72 – 74	3	Thiamine pyrophosphate binding By similarity
	Region	107 – 110	4	Substrate binding By similarity
	Region	123 – 125	3	Thiamine pyrophosphate binding By similarity
	Region	153 – 159	7	Thiamine pyrophosphate binding By similarity
	Region	183 – 187	5	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	154	1	Magnesium By similarity
	Metal binding	183	1	Magnesium By similarity
	Metal binding	185	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	44	1	Substrate By similarity
	Binding site	73	1	Substrate By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	252	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37940-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 39584D3F4363E656	FASTA	330	36,334
	10 20 30 40 50 60 MSTNRHQALG LTDQEAVDMY RTMLLARKID ERMWLLNRSG KIPFVISCQG QEAAQVGAAF 70 80 90 100 110 120 ALDREMDYVL PYYRDMGVVL AFGMTAKDLM MSGFAKAADP NSGGRQMPGH FGQKKNRIVT 130 140 150 160 170 180 GSSPVTTQVP HAVGIALAGR MEKKDIAAFV TFGEGSSNQG DFHEGANFAA VHKLPVIFMC 190 200 210 220 230 240 ENNKYAISVP YDKQVACENI SDRAIGYGMP GVTVNGNDPL EVYQAVKEAR ERARRGEGPT 250 260 270 280 290 300 LIETISYRLT PHSSDDDDSS YRGREEVEEA KKSDPLLTYQ AYLKETGLLS DEIEQTMLDE 310 320 330 IMAIVNEATD EAENAPYAAP ESALDYVYAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of branched-chain alpha-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other alpha-oxo acid dehydrogenases." Wang G.-F., Kuriki T., Roy K.L., Kaneda T. Eur. J. Biochem. 213:1091-1099(1993) [PubMed: 8504804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22. Strain: 168.
[2]	"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M97391 Genomic DNA. Translation: AAA22278.1. D84432 Genomic DNA. Translation: BAA12598.1. Z99116 Genomic DNA. Translation: CAB14336.1.
PIR	C69593.
RefSeq	NP_390285.1.
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P12694.
ModBase	Search...
Genome annotation databases
GeneID	938674.
GenomeReviews	Gene locus BSU24050 in contig AL009126_GR.
KEGG	bsu:BSU24050.
NMPDR	fig|224308.1.peg.2409.
Organism-specific databases
SubtiList	BG10307. bfmBAA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P37940.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2403-MON. MetaCyc:MON-11683.
Family and domain databases
InterPro	IPR001017. DHase_E1. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODBA_BACSU

Accession

Primary (citable) accession number: P37940

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 4, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)