P23129 (ODO1_BACSU) Reviewed, UniProtKB/Swiss-Prot

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 (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	944 AA.
Sequence status	Complete.
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-Rule MF_01169
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. HAMAP-Rule MF_01169
Cofactor	Thiamine pyrophosphate.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Molecular_function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: HAMAP thiamine 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 – 944	944	2-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169		PRO_0000162169
Experimental info
	Sequence conflict	35	1	N → Y in CAA38576. Ref.1
	Sequence conflict	110	1	L → S in AAC17864. Ref.5
	Sequence conflict	133	1	P → L in AAC17864. Ref.5
	Sequence conflict	231	1	I → T in AAC17864. Ref.5
	Sequence conflict	275 – 277	3	NKD → RS in CAA38576. Ref.1
	Sequence conflict	283 – 316	34	GSIGI…SARIT → DPLESATDGRGMSNTIWGRI GSFKTLKQNQPALP in CAA38576. Ref.1
	Sequence conflict	488 – 494	7	VKQIFAE → SNKFSLK in CAA38576. Ref.1
	Sequence conflict	520 – 522	3	DAY → VAI in CAA38576. Ref.1
	Sequence conflict	554 – 556	3	DFD → HFH in CAA38576. Ref.1
	Sequence conflict	567 – 569	3	NWP → TG in CAA38576. Ref.1
	Sequence conflict	573 – 585	13	NVFGK…ILERR → MFSQAKAHFRKT in CAA38576. Ref.1
	Sequence conflict	837 – 838	2	SD → DV in AAA22628. Ref.6
	Sequence conflict	838	1	D → V in CAA38576. Ref.1
	Sequence conflict	927 – 944	18	VHKKE…LTRKN → EFIKKNRNVLYLIA in CAA38576. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23129 [UniParc]. Last modified July 28, 2009. Version 3. Checksum: DCBC7B28C44A9CC2	FASTA	944	106,278
	10 20 30 40 50 60 MFQNSMKQRM NWEDFYGPNL GYALELYDQY TQDPNSIDPD 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 QHAPNKDLVP SEGSIGISYG WTGDVKYHLG 310 320 330 340 350 360 ANRELQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQSGYPVQ DETKSLAILI 370 380 390 400 410 420 HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF TTESAESRST KYASDLAKGY 430 440 450 460 470 480 EIPIVHVNAD DPEACLSAVK FAVEYRKTFN KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD 490 500 510 520 530 540 AVRKHPTVKQ IFAEKLVKEG VVTEEVVQNI EKSVTKRIED AYQKVPSKKE HTACEIELPE 550 560 570 580 590 600 PVSNGFPDVD TSIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA 610 620 630 640 650 660 ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG KEFVPLHHLS DCSTSFAVHN 670 680 690 700 710 720 SPLSEGSVLG FEYGYNVHSP ETLVLWEAQY GDFANAAQVY FDQFISAGRA KWGQKSGLVM 730 740 750 760 770 780 LLPHGYEGQG PEHSSGRIER FLQLAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL 790 800 810 820 830 840 VIMTPKSLLR NPNTVSEVQE LSESRFQPVY EQSGLSHDYE KVTRLVLSSG KVSIDISDHF 850 860 870 880 890 900 NKLEDGKEWL HIARIEQLYP FPAKGVKELF AKLPNLKEIV WVQEEPQNMG AWGYISPYLT 910 920 930 940 EIAPEGVSVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270. Strain: 168.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-944. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X54805 Genomic DNA. Translation: CAA38576.1. AL009126 Genomic DNA. Translation: CAB13829.3. AF026147 Genomic DNA. Translation: AAC17864.1. M27141 Genomic DNA. Translation: AAA22628.1.
PIR	A32879. S25295.
RefSeq	NP_389819.3. NC_000964.3.
3D structure databases
ProteinModelPortal	P23129.
SMR	P23129. Positions 71-943.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU19370.
Proteomic databases
PaxDb	P23129.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB13829; CAB13829; BSU19370.
GeneID	939507.
KEGG	bsu:BSU19370.
PATRIC	18975725. VBIBacSub10457_2053.
Organism-specific databases
GenoList	BSU19370. [Micado]
Phylogenomic databases
eggNOG	COG0567.
HOGENOM	HOG000259588.
KO	K00164.
ProtClustDB	PRK09404.
Enzyme and pathway databases
BioCyc	BSUB:BSU19370-MONOMER.
Family and domain databases
HAMAP	MF_01169. SucA_OdhA.
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR023784. 2oxoglutarate_DH_E1_bac. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. PTHR23152. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
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:	July 28, 2009
Last modified:	May 1, 2013
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program