sucB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

SucB

Synonyms

dihydrolipoyl transsuccinase[1], B0727[2][1] , ECK0715, JW0716, b0727

Product description

SucB-lipoate[2][3]

SucB-S-succinyldihydrolipoate

2-oxoglutarate dehydrogenase, E2 component; dihydrolipoamide succinyltransferase; acid-inducible; yields succinyl-CoA and CO(2)[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology

SucB-lipoate

See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0004149

dihydrolipoyllysine-residue succinyltransferase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006255

F

Seeded from EcoCyc (v14.0)

complete

GO:0004149

dihydrolipoyllysine-residue succinyltransferase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.3.1.61

F

Seeded from EcoCyc (v14.0)

complete

GO:0045252

oxoglutarate dehydrogenase complex

PMID:5335914[5]

IDA: Inferred from Direct Assay

C

complete

GO:0005488

binding

PMID:6365919[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0006099

tricarboxylic acid cycle

PMID:6284701[7]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004149

dihydrolipoyllysine-residue succinyltransferase activity

PMID:6284701[7]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005515

protein binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004167

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:5335915[8]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0004149

dihydrolipoyllysine-residue succinyltransferase activity

PMID:5335914[5]

IDA: Inferred from Direct Assay

F

complete

GO:0006099

tricarboxylic acid cycle

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006255

P

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:5335915[8]

IDA: Inferred from Direct Assay

F

Dihydrolipoyl transacetylase has 24 monomers of SucB.

complete

GO:0006099

tricarboxylic acid cycle

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0816

P

Seeded from EcoCyc (v14.0)

complete

GO:0031405

lipoic acid binding

PMID:1854331[9]

IDA: Inferred from Direct Assay

F

complete

GO:0031405

lipoic acid binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0450

F

Seeded from EcoCyc (v14.0)

complete

GO:0005488

binding

PMID:6365919[6]

IDA: Inferred from Direct Assay

F

3-bromopyruvate inactivates pyruvate dehydrogenase activity (Figure 1).

complete

GO:0045252

oxoglutarate dehydrogenase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006255

C

Seeded from EcoCyc (v14.0)

complete

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Interactions

SucB-lipoate

See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

lpdA

PMID:15690043[10]

Experiment(s):EBI-880739

Protein

ycgL

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

fur

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

rtcB

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

pqiA

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

lipA

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

yciH

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

mreB

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

dnaE

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

ftsZ

PMID:16606699[11]

Experiment(s):EBI-1137807

Protein

ybaY

PMID:15690043[10]

Experiment(s):EBI-886840

Protein

ybaY

PMID:19402753[12]

LCMS(ID Probability):99.0

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

Cytoplasm

PMID:9298646[13]

EchoLocation:sucB


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MSSVDILVPD LPESVADATV ATWHKKPGDA VVRDEVLVEI ETDKVVLEVP ASADGILDAV
LEDEGTTVTS RQILGRLREG NSAGKETSAK SEEKASTPAQ RQQASLEEQN NDALSPAIRR
LLAEHNLDAS AIKGTGVGGR LTREDVEKHL AKAPAKESAP AAAAPAAQPA LAARSEKRVP
MTRLRKRVAE RLLEAKNSTA MLTTFNEVNM KPIMDLRKQY GEAFEKRHGI RLGFMSFYVK
AVVEALKRYP EVNASIDGDD VVYHNYFDVS MAVSTPRGLV TPVLRDVDTL GMADIEKKIK
ELAVKGRDGK LTVEDLTGGN FTITNGGVFG SLMSTPIINP PQSAILGMHA IKDRPMAVNG
QVEILPMMYL ALSYDHRLID GRESVGFLVT IKELLEDPTR LLLDV
Length

405

Mol. Wt

44.011 kDa

pI

5.7 (calculated)

Extinction coefficient

15,930 (calc based on 7 Y, 1 W, and 0 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P0AFG6

Domain

173..403

PF00198 2-oxoacid dehydrogenases acyltransferase (catalytic domain)

PMID:19920124[14]

Domain

4..77

PF00364 Biotin-requiring enzyme

PMID:19920124[14]

Domain

111..148

PF02817 e3 binding domain

PMID:19920124[14]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=sucB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128702

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945307

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0002480

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0AFG6

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10980

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10980

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945307

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000969

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0973

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 Willms, CR et al. (1967) Alpha-keto acid dehydrogenase complexes. VI. Dissociation and reconstitution of the dihydrolipoyl transacetylase of Escherichia coli. J. Biol. Chem. 242 889-97 PubMed
  6. ↑ 6.0 6.1 Apfel, MA et al. (1984) Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate. J. Biol. Chem. 259 2905-9 PubMed
  7. ↑ 7.0 7.1 Spencer, ME & Guest, JR (1982) Molecular cloning of four tricarboxylic acid cyclic genes of Escherichia coli. J. Bacteriol. 151 542-52 PubMed
  8. ↑ 8.0 8.1 Henney, HR Jr et al. (1967) Alpha-keto acid dehydrogenase complexes. VII. Isolation and partial characterization of the polypeptide chains in the dihydrolipoyl transacetylase of Escherichia coli. J. Biol. Chem. 242 898-901 PubMed
  9. ↑ Packman, LC et al. (1991) Lipoylation of the E2 components of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli. Biochem. J. 277 ( Pt 1) 153-8 PubMed
  10. ↑ 10.0 10.1 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 11.4 11.5 11.6 11.7 11.8 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  12. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  13. ↑ Link, AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 1259-313 PubMed
  14. ↑ 14.0 14.1 14.2 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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