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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

odhB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).

Catalytic activityi

Succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi: L-lysine degradation via saccharopine pathway

This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (odhB)
This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei388By similarity1
Active sitei392By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyciBSUB:BSU19360-MONOMER
BRENDAi2.3.1.61 658
UniPathwayiUPA00868; UER00840

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene namesi
Name:odhB
Synonyms:citM
Ordered Locus Names:BSU19360
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622561 – 417Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexAdd BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42N6-lipoyllysinePROSITE-ProRule annotation1

Proteomic databases

PaxDbiP16263
PRIDEiP16263

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010686

Structurei

3D structure databases

ProteinModelPortaliP16263
SMRiP16263
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 76Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini123 – 160Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA
HOGENOMiHOG000281563
InParanoidiP16263
KOiK00658
OMAiMKVPSPG
PhylomeDBiP16263

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
IPR006255 SucB
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01347 sucB, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

P16263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEIKVPELA ESISEGTIAQ WLKQPGDYVE QGEYLLELET DKVNVELTAE
60 70 80 90 100
ESGVLQEVLK DSGDTVQVGE IIGTISEGAG ESSAPAPTEK TESKESVKEE
110 120 130 140 150
KQAEPAAQEV SEEAQSEAKS RTIASPSARK LAREKGIDLS QVPTGDPLGR
160 170 180 190 200
VRKQDVEAYE KPASKPAPQQ KQQPQAQKAQ QSFDKPVEVQ KMSRRRQTIA
210 220 230 240 250
KRLVEVQQTS AMLTTFNEVD MTAVMNLRKR RKDQFFEQNE VKLGFMSFFT
260 270 280 290 300
KAVVAALKKY PLLNAEIQGD ELIVKKFYDI GIAVAADEGL VVPVVRDADR
310 320 330 340 350
LTFAGIEKEI GELAKKARNN KLTLSELQGG SFTITNGGTF GSLMSTPILN
360 370 380 390 400
SPQVGILGMH KIQLRPVAID EERFENRPMM YIALSYDHRI VDGKEAVGFL
410
VTIKNLLEDP EQLLLEG
Length:417
Mass (Da):46,003
Last modified:July 7, 2009 - v2
Checksum:iE736FF4383B1A966
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti287D → V in AAA22629 (PubMed:2500417).Curated1
Sequence conflicti328Q → E in AAA22629 (PubMed:2500417).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27141 Genomic DNA Translation: AAA22629.1
AL009126 Genomic DNA Translation: CAB13828.2
PIRiB32879
RefSeqiNP_389818.2, NC_000964.3
WP_004399364.1, NZ_JNCM01000036.1

Genome annotation databases

EnsemblBacteriaiCAB13828; CAB13828; BSU19360
GeneIDi939505
KEGGibsu:BSU19360
PATRICifig|224308.179.peg.2117

Similar proteinsi

Entry informationi

Entry nameiODO2_BACSU
AccessioniPrimary (citable) accession number: P16263
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 7, 2009
Last modified: March 28, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health