accD: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

AccD

Synonyms

acetyl-CoA carboxylase, beta (carboxyltranferase) subunit[1], B2316[2][1], DedB[2][1], AccD[2][1] , dedB, ECK2310, JW2313, usg, b2316

Product description

AccD[2][3];

Component of carboxyl transferase subunit β[2][3]; acetyl-CoA carboxyltransferase[2][3]; acetyl CoA carboxylase[2][3]

Acetyl-CoA carboxylase, carboxyltransferase beta subunit[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:0000166

nucleotide binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc (v14.0)

complete

GO:0003677

DNA binding

PMID:19965770[5]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc (v14.0)

complete

GO:0003729

mRNA binding

PMID:19965770[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0003989

acetyl-CoA carboxylase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01395

F

Seeded from EcoCyc (v14.0)

complete

GO:0003989

acetyl-CoA carboxylase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000438

F

Seeded from EcoCyc (v14.0)

complete

GO:0003989

acetyl-CoA carboxylase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:6.4.1.2

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:15690043[6]

IPI: Inferred from Physical Interaction

UniProtKB:P0ABD5

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0006633

fatty acid biosynthetic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01395

P

Seeded from EcoCyc (v14.0)

complete

GO:0006633

fatty acid biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000438

P

Seeded from EcoCyc (v14.0)

complete

GO:0006633

fatty acid biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0275

P

Seeded from EcoCyc (v14.0)

complete

GO:0006633

fatty acid biosynthetic process

PMID:10893421[8]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0862

F

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

PMID:16460018[9]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

PMID:19965770[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0009329

acetate CoA-transferase complex

PMID:1355089[10]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0016874

ligase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000022

F

Seeded from EcoCyc (v14.0)

complete

GO:0016874

ligase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011762

F

Seeded from EcoCyc (v14.0)

complete

GO:0016874

ligase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0436

F

Seeded from EcoCyc (v14.0)

complete

GO:0017148

negative regulation of translation

PMID:19965770[5]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc (v14.0)

complete

GO:0003989

acetyl-CoA carboxylase activity

PMID:10893421[8]

IDA: Inferred from Direct Assay

F

complete

GO:0006633

fatty acid biosynthetic process

PMID:10893421[8]

IGI: Inferred from Genetic Interaction

EcoliWiki:accA EcoliWiki:accB EcoliWiki:accC


P

complete

GO:0042759

long-chain fatty acid biosynthetic process

PMID:18156466[11]

NAS: Non-traceable Author Statement

P

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 carboxyl transferase subunit β

could be indirect

Protein

dnaK

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

pepD

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

pgm

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

rfaI

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

rplU

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

rplV

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

rpmG

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

mdtB

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

yhdA

PMID:15690043[6]

Experiment(s):EBI-890114

Protein

accA

PMID:19402753[12]

LCMS(ID Probability):99.0 MALDI(Z-score):17.053160

Protein

Subunits of acetyl-CoA carboxyltransferase

could be indirect

Protein

Subunits of acetyl CoA carboxylase

could be indirect


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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 

MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD HHMRMTARNR
LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK ETGEKDALVV MKGTLYGMPV
VAAAFEFAFM GGSMGSVVGA RFVRAVEQAL EDNCPLICFS ASGGARMQEA LMSLMQMAKT
SAALAKMQER GLPYISVLTD PTMGGVSASF AMLGDLNIAE PKALIGFAGP RVIEQTVREK
LPPGFQRSEF LIEKGAIDMI VRRPEMRLKL ASILAKLMNL PAPNPEAPRE GVVVPPVPDQ EPEA
Length

304

Mol. Wt

33.322 kDa

pI

7.7 (calculated)

Extinction coefficient

16,960 - 17,710 (calc based on 4 Y, 2 W, and 6 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

51..302

PF01039 Carboxyl transferase domain

PMID:19920124[13]

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

Structures

<beststructure> gene=accD 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:16130251

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946796

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0007648

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A9Q5

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10217

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10217

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946796

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000211

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0213

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 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 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 5.2 5.3 Meades, G Jr et al. (2010) A tale of two functions: enzymatic activity and translational repression by carboxyltransferase. Nucleic Acids Res. 38 1217-27 PubMed
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 6.6 6.7 6.8 6.9 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  7. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  8. ↑ 8.0 8.1 8.2 Davis, MS et al. (2000) Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli. J. Biol. Chem. 275 28593-8 PubMed
  9. ↑ Bilder, P et al. (2006) The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry 45 1712-22 PubMed
  10. ↑ Li, SJ & Cronan, JE Jr (1992) The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267 16841-7 PubMed
  11. ↑ Benson, BK et al. (2008) DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: implications for active site communication. Protein Sci. 17 34-42 PubMed
  12. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  13. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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