Reviewed, UniProtKB/Swiss-Prot P23129 (ODO1_BACSU)

Names and origin

Protein names

Recommended name:
    2-oxoglutarate dehydrogenase E1 component
    EC=1.2.4.2
Alternative name(s):
    Alpha-ketoglutarate dehydrogenase

Gene names

Name:	odhA
Synonyms:	citK
Ordered Locus Names:	BSU19370

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	941 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). HAMAP MF_01169
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. HAMAP MF_01169
Cofactor	Thiamine pyrophosphate. HAMAP MF_01169
Subunit structure	Homodimer. HAMAP MF_01169
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: HAMAP thiamin pyrophosphate binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 941	941	2-oxoglutarate dehydrogenase E1 component HAMAP MF_01169		PRO_0000162169
Experimental info
	Sequence conflict	35	1	Y → N in AAC17864. Ref.4
	Sequence conflict	110	1	L → S in AAC17864. Ref.4
	Sequence conflict	133	1	P → L in AAC17864. Ref.4
	Sequence conflict	231	1	I → T in AAC17864. Ref.4
	Sequence conflict	834	1	S → D in AAA22628. Ref.5
	Sequence conflict	924 – 941	18	VHKKE…LTRKN → EFIKKNRNVLYLIA in CAA38576. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23129-1 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: 6B2D1CE12572E7C4	FASTA	941	105,740
	10 20 30 40 50 60 MFQNSMKQRM NWEDFYGPNL GYALELYDQY TQDPYSIDPD LKEMFDELGA PPSDIKEASG 70 80 90 100 110 120 TKEKGRVTAD LIQKIASAVR LAEDIRTYGH LNASVNPLRK DEKKSELFPL SDYGLTEEEI 130 140 150 160 170 180 KAIPASVICK DAPKNISNGL EAIQYLRNTY KRTISFEFDH VHDFKEREWL TRKIESGELF 190 200 210 220 230 240 QKNSAEKLSA VLERLTEVEG FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKSGTT 250 260 270 280 290 300 SVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPRSLVPS EDPLESATDG RGMSNTIWGR 310 320 330 340 350 360 IGSFKTLKQN QPALPLANNP SHLEFINPIV EGSTRAAQET RTQSGYPVQD ETKSLAILIH 370 380 390 400 410 420 GDAAFPGEGI VAETLNLSSL KGYQVGGAIH IIANNMIGFT TESAESRSTK YASDLAKGYE 430 440 450 460 470 480 IPIVHVNADD PEACLSAVKF AVEYRKTFNK DFLIDLIGYR RYGHNEMDEP STTQPMLYDA 490 500 510 520 530 540 VRKHPTSNKF SLKKLVKEGV VTEEVVQNIE KSVTKRIEVA IQKVPSKKEH TACEIELPEP 550 560 570 580 590 600 VSNGFPDVDT SIHFHVLRKL NGELITGESF MFSQAKAHFR KTAKAFDDDR KVEWSLAESL 610 620 630 640 650 660 AFASILKDGT PIRLTGQDSE RGTFAQRNLV LHDSETGKEF VPLHHLSDCS TSFAVHNSPL 670 680 690 700 710 720 SEGSVLGFEY GYNVHSPETL VLWEAQYGDF ANAAQVYFDQ FISAGRAKWG QKSGLVMLLP 730 740 750 760 770 780 HGYEGQGPEH SSGRIERFLQ LAAENNWTVA NLTSAAQYFH ILRRQAKMLL REEIRPLVIM 790 800 810 820 830 840 TPKSLLRNPN TVSEVQELSE SRFQPVYEQS GLSHDYEKVT RLVLSSGKVS IDISVHFNKL 850 860 870 880 890 900 EDGKEWLHIA RIEQLYPFPA KGVKELFAKL PNLKEIVWVQ EEPQNMGAWG YISPYLTEIA 910 920 930 940 PEGVSVQYIG RRRRSSPAEG DPTVHKKEQE RIVSDSLTRK N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex." Resnekov O., Melin L., Carlsson P., Mannerloev M., von Gabain A., Hederstedt L. Mol. Gen. Genet. 234:285-296(1992) [PubMed: 1508153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"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.
[3]	"Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence." Medigue C., Rose M., Viari A., Danchin A. Genome Res. 9:1116-1127(1999) [PubMed: 10568751] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"Sequence analysis of the Bacillus subtilis 168 chromosome region between the sspC and odhA loci (184 degrees-180 degrees)." Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D., Park S.-H. DNA Res. 5:195-201(1998) [PubMed: 9734814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270. Strain: 168.
[5]	"Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively." Carlsson P., Hederstedt L. J. Bacteriol. 171:3667-3672(1989) [PubMed: 2500417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 649-941. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X54805 Genomic DNA. Translation: CAA38576.1. Z99114 Genomic DNA. Translation: CAB13829.2. AF026147 Genomic DNA. Translation: AAC17864.1. M27141 Genomic DNA. Translation: AAA22628.1.
PIR	A32879. S25295.
RefSeq	NP_389819.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	939507.
GenomeReviews	Gene locus BSU19370 in contig AL009126_GR.
KEGG	bsu:BSU19370.
Organism-specific databases
SubtiList	BG10272. odhA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P23129.
OMA	P23129. EGDEPAF.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1937-MON.
BRENDA	1.2.4.2. 150.
Family and domain databases
HAMAP	MF_01169. [Tree]
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase_central-reg. [Graphical view]
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODO1_BACSU

Accession

Primary (citable) accession number: P23129
Secondary accession number(s): O68261, Q45642

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	August 31, 2004
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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