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P0AFG7

- ODO2_ECO57

UniProt

P0AFG7 - ODO2_ECO57

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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

sucB

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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) (By similarity).By similarity

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei376 – 3761By similarity
Active sitei380 – 3801By similarity

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciECOL386585:GJFA-747-MONOMER.
ECOO157:SUCB-MONOMER.
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:sucB
Ordered Locus Names:Z0881, ECs0752
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 405404Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000162263Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-lipoyllysineBy similarityPROSITE-ProRule annotation
Modified residuei148 – 1481N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP0AFG7.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Protein-protein interaction databases

MINTiMINT-1242594.
STRINGi155864.Z0881.

Structurei

Secondary structure

1
405
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi118 – 1258Combined sources
Helixi129 – 1313Combined sources
Beta strandi136 – 1394Combined sources
Helixi143 – 1497Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CYUNMR-A113-152[»]
ProteinModelPortaliP0AFG7.
SMRiP0AFG7. Positions 2-81, 104-153, 173-405.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFG7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7876Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiMMSTPIV.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AFG7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSVDILVPD LPESVADATV ATWHKKPGDA VVRDEVLVEI ETDKVVLEVP
60 70 80 90 100
ASADGILDAV LEDEGTTVTS RQILGRLREG NSAGKETSAK SEEKASTPAQ
110 120 130 140 150
RQQASLEEQN NDALSPAIRR LLAEHNLDAS AIKGTGVGGR LTREDVEKHL
160 170 180 190 200
AKAPAKESAP AAAAPAAQPA LAARSEKRVP MTRLRKRVAE RLLEAKNSTA
210 220 230 240 250
MLTTFNEVNM KPIMDLRKQY GEAFEKRHGI RLGFMSFYVK AVVEALKRYP
260 270 280 290 300
EVNASIDGDD VVYHNYFDVS MAVSTPRGLV TPVLRDVDTL GMADIEKKIK
310 320 330 340 350
ELAVKGRDGK LTVEDLTGGN FTITNGGVFG SLMSTPIINP PQSAILGMHA
360 370 380 390 400
IKDRPMAVNG QVEILPMMYL ALSYDHRLID GRESVGFLVT IKELLEDPTR

LLLDV
Length:405
Mass (Da):44,011
Last modified:January 23, 2007 - v2
Checksum:i8439E48C6D381277
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG55051.1.
BA000007 Genomic DNA. Translation: BAB34175.1.
PIRiG85573.
H90722.
RefSeqiNP_286443.1. NC_002655.2.
NP_308779.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG55051; AAG55051; Z0881.
BAB34175; BAB34175; BAB34175.
GeneIDi917484.
957834.
KEGGiece:Z0881.
ecs:ECs0752.
PATRICi18350526. VBIEscCol44059_0774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG55051.1 .
BA000007 Genomic DNA. Translation: BAB34175.1 .
PIRi G85573.
H90722.
RefSeqi NP_286443.1. NC_002655.2.
NP_308779.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CYU NMR - A 113-152 [» ]
ProteinModelPortali P0AFG7.
SMRi P0AFG7. Positions 2-81, 104-153, 173-405.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1242594.
STRINGi 155864.Z0881.

Proteomic databases

PRIDEi P0AFG7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG55051 ; AAG55051 ; Z0881 .
BAB34175 ; BAB34175 ; BAB34175 .
GeneIDi 917484.
957834.
KEGGi ece:Z0881.
ecs:ECs0752.
PATRICi 18350526. VBIEscCol44059_0774.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281563.
KOi K00658.
OMAi MMSTPIV.
OrthoDBi EOG610413.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .
BioCyci ECOL386585:GJFA-747-MONOMER.
ECOO157:SUCB-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AFG7.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01347. sucB. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiODO2_ECO57
AccessioniPrimary (citable) accession number: P0AFG7
Secondary accession number(s): P07016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3