fadD: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

FadD

Synonyms

acyl-CoA synthetase (long-chain-fatty-acid--CoA ligase)[1], B1805[2][1], OldD[2][1], FadD[2][1] , ECK1803, JW1794, oldD, b1805

Product description

FadD[2][3];

Component of fatty acyl-CoA synthetase[2][3]

Acyl-CoA synthase[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:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

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:0004467

long-chain fatty acid-CoA ligase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:6.2.1.3

F

Seeded from EcoCyc (v14.0)

complete

GO:0004467

long-chain fatty acid-CoA ligase activity

PMID:7016858[5]

IDA: Inferred from Direct Assay

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:12034706[6]

TAS: Traceable Author Statement

C

Seeded from EcoCyc (v14.0)

complete

GO:0006635

fatty acid beta-oxidation

PMID:7016858[5]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc (v14.0)

complete

GO:0006637

acyl-CoA metabolic process

PMID:7016858[5]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc (v14.0)

complete

GO:0009898

internal side of plasma membrane

PMID:12034706[6]

TAS: Traceable Author Statement

C

Seeded from EcoCyc (v14.0)

complete

GO:0019898

extrinsic to membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-9903

C

Seeded from EcoCyc (v14.0)

complete

GO:0004467

long-chain fatty acid-CoA ligase activity

PMID:1460045[7]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0006631

fatty acid metabolic process

PMID:1649829[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0008654

phospholipid biosynthetic process

PMID:1649829[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0006629

lipid metabolic process

PMID:1649829[8]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0005504

fatty acid binding

PMID:9030548[9]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0004467

long-chain fatty acid-CoA ligase activity

PMID:9030548[9]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0070538

oleic acid binding

PMID:9030548[9]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005737

cytoplasm

PMID:9030548[9]

IDA: Inferred from Direct Assay

C

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 fatty acyl-CoA synthetase

could be indirect

Protein

cysI

PMID:16606699[10]

Experiment(s):EBI-1140873

Protein

hyaB

PMID:16606699[10]

Experiment(s):EBI-1140873

Protein

mnmG

PMID:16606699[10]

Experiment(s):EBI-1140873

Protein

insL1

PMID:16606699[10]

Experiment(s):EBI-1140873, EBI-1140873

Protein

groL

PMID:16606699[10]

Experiment(s):EBI-1140873

Protein

sdhA

PMID:16606699[10]

Experiment(s):EBI-1140873
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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 

MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT FRKLEERSRA
FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI VVNVNPLYTP RELEHQLNDS
GASAIVIVSN FAHTLEKVVD KTAVQHVILT RMGDQLSTAK GTVVNFVVKY IKRLVPKYHL
PDAISFRSAL HNGYRMQYVK PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA
TYGPLLHPGK ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF
TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG QYLLEGYGLT
ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVP PGQPGELCVK GPQVMLGYWQ
RPDATDEIIK NGWLHTGDIA VMDEEGFLRI VDRKKDMILV SGFNVYPNEI EDVVMQHPGV
QEVAAVGVPS GSSGEAVKIF VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN
VGKILRRELR DEARGKVDNK A
Length

561

Mol. Wt

62.331 kDa

pI

6.7 (calculated)

Extinction coefficient

53,290 - 53,790 (calc based on 21 Y, 4 W, and 4 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

50..485

PF00501 AMP-binding enzyme

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=fadD 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:16129759

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946327

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0006005

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P69451

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11530

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11530

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946327

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001484

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1492

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 1.5 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 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 Kameda, K & Nunn, WD (1981) Purification and characterization of acyl coenzyme A synthetase from Escherichia coli. J. Biol. Chem. 256 5702-7 PubMed
  6. ↑ 6.0 6.1 Weimar, JD et al. (2002) Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. J. Biol. Chem. 277 29369-76 PubMed
  7. ↑ Black, PN et al. (1992) Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase. J. Biol. Chem. 267 25513-20 PubMed
  8. ↑ 8.0 8.1 8.2 Hsu, L et al. (1991) Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity. J. Biol. Chem. 266 13783-8 PubMed
  9. ↑ 9.0 9.1 9.2 9.3 Black, PN et al. (1997) Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. J. Biol. Chem. 272 4896-903 PubMed
  10. ↑ 10.0 10.1 10.2 10.3 10.4 10.5 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  11. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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