lipA: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

LipA

Synonyms

lipoate synthase[1], B0628[2][1], Lip[2][1], LipA[2][1] , ECK0621, JW0623, lip, b0628

Product description

lipoate synthase[2][3];

Component of lipoate synthase[3]

Lipoyl synthase, iron-sulfur protein; SAM-dependent chemistry[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
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:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007197

F

Seeded from EcoCyc (v14.0)

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

F

Seeded from EcoCyc (v14.0)

complete

GO:0005506

iron ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0408

F

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00206

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded from EcoCyc (v14.0)

complete

GO:0008152

metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

P

Seeded from EcoCyc (v14.0)

complete

GO:0016992

lipoate synthase activity

PMID:15157071[5]

IDA: Inferred from Direct Assay

F

complete

GO:0009107

lipoate biosynthetic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00206

P

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:15157071[5]

IDA: Inferred from Direct Assay

C

complete

GO:0009107

lipoate biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003698

P

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:10747808[6]

IDA: Inferred from Direct Assay

F

complete

GO:0016740

transferase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0808

F

Seeded from EcoCyc (v14.0)

complete

GO:0009249

protein lipoylation

PMID:15157071[5]

IDA: Inferred from Direct Assay

P

complete

GO:0016992

lipoate synthase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00206

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:11106496[7]

IPI: Inferred from Physical Interaction

F

LipA is monomeric and homodimeric.

Missing: with/from

GO:0016992

lipoate synthase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003698

F

Seeded from EcoCyc (v14.0)

complete

GO:0009107

lipoate biosynthetic process

PMID:8444795[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0016992

lipoate synthase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.8.1.8

F

Seeded from EcoCyc (v14.0)

complete

GO:0046872

metal ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc (v14.0)

complete

GO:0051536

iron-sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007197

F

Seeded from EcoCyc (v14.0)

complete

GO:0051536

iron-sulfur cluster binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0411

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00206

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003698

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0004

F

Seeded from EcoCyc (v14.0)

complete

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Interactions 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

Subunits of lipoate synthase

could be indirect

Protein

yibL

PMID:16606699[9]

Experiment(s):EBI-1137482

Protein

nadE

PMID:16606699[9]

Experiment(s):EBI-1137482

Protein

groL

PMID:16606699[9]

Experiment(s):EBI-1137482

Protein

ybaQ

PMID:16606699[9]

Experiment(s):EBI-1137482

Protein

gabT

PMID:16606699[9]

Experiment(s):EBI-1137482

Protein

tatE

PMID:16606699[9]

Experiment(s):EBI-1137482

Protein

dnaK

PMID:16606699[9]

Experiment(s):EBI-1137482

Protein

groS

PMID:19402753[10]

MALDI(Z-score):24.533555

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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
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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 

MSKPIVMERG VKYRDADKMA LIPVKNVATE REALLRKPEW MKIKLPADST RIQGIKAAMR
KNGLHSVCEE ASCPNLAECF NHGTATFMIL GAICTRRCPF CDVAHGRPVA PDANEPVKLA
QTIADMALRY VVITSVDRDD LRDGGAQHFA DCITAIREKS PQIKIETLVP DFRGRMDRAL
DILTATPPDV FNHNLENVPR IYRQVRPGAD YNWSLKLLER FKEAHPEIPT KSGLMVGLGE
TNEEIIEVMR DLRRHGVTML TLGQYLQPSR HHLPVQRYVS PDEFDEMKAE ALAMGFTHAA
CGPFVRSSYH ADLQAKGMEV K
Length

321

Mol. Wt

36.071 kDa

pI

8.0 (calculated)

Extinction coefficient

21,430 - 22,430 (calc based on 7 Y, 2 W, and 8 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

Domain

88..252

PF04055 Radical SAM superfamily

PMID:19920124[11]

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

Structures

<beststructure> gene=lipA 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:16128611

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945227

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0002155

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P60716

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11306

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11306

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945227

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001279

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1283

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 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 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 5.2 Cicchillo, RM et al. (2004) Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. Biochemistry 43 6378-86 PubMed
  6. ↑ Ollagnier-De Choudens, S et al. (2000) Iron-sulfur center of biotin synthase and lipoate synthase. Biochemistry 39 4165-73 PubMed
  7. ↑ Miller, JR et al. (2000) Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 39 15166-78 PubMed
  8. ↑ Reed, KE & Cronan, JE Jr (1993) Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes. J. Bacteriol. 175 1325-36 PubMed
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 9.6 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  10. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  11. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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