fabI:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

FabI product

Synonyms

enoyl-[acyl-carrier-protein] reductase, NADH-dependent product[1], B1288 product[2][1], Gts product[2][1], QmeA product[2][1], EnvM product[2][1], FabI product[2][1]

Product description

ENOYL-ACP-REDUCT-NADH-MONOMER[2][3]

EC number (for enzymes)
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Notes

Function

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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(s) Evidence Code with/from Aspect Notes Status
GO:0004318

enoyl-(acyl-carrier-protein) reductase (NADH) activity

GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.3.1.9

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[5]

IPI: Inferred from Physical Interaction

UniProtKB:P0AF90

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005624

membrane fraction

PMID:16858726[6]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0006633

fatty acid biosynthetic process

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0275

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002198

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002347

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0008610

lipid biosynthetic process

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0444

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0397

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0016491

oxidoreductase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002198

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0016491

oxidoreductase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002347

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0016491

oxidoreductase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

C

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006654

phosphatidic acid biosynthetic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0046677

response to antibiotic

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0046

P

Seeded from EcoCyc 12.5 [4]

complete

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Interactions

Partner Type Partner Notes
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Notes

Localization

Compartment Description Evidence Notes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc 

MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSDIV
LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKIAHDIS
SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE
GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI
SGEVVHVDGG FSIAAMNELE LK
Mol. Wt

27.86 kDa (calc) [2]

pI

5.88[2]

Extinction coefficient

15930 - 16430 (calc based on 7 Y, 1 W, and 4 C residues)

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Domains/Motifs/Modification Sites

Type Residues Description Notes
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Structure

Structure Type Organism Accession Residues covered Notes

X-RAY DIFFRACTION

Escherichia coli

1MFP E. coli Enoyl Reductase in complex with NAD and SB611113

X-RAY DIFFRACTION

Escherichia coli

1QSG CRYSTAL STRUCTURE OF ENOYL REDUCTASE INHIBITION BY TRICLOSAN

X-RAY DIFFRACTION

Escherichia coli

1I30 E. COLI ENOYL REDUCTASE +NAD+SB385826

X-RAY DIFFRACTION

Escherichia coli

1I2Z E. COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND BRL-12654

X-RAY DIFFRACTION

Escherichia coli

1DFI X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD

X-RAY DIFFRACTION

Escherichia coli

1DFH X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE

X-RAY DIFFRACTION

Escherichia coli

1DFG X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND BENZO-DIAZABORINE

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Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER

SwissModel (EcoliWiki Page)

SwissModel:P0AEK4

UniProt (EcoliWiki Page)

UniProt:P0AEK4

PFAM (EcoliWiki Page)

PFAM:PF00106

RefSeq (EcoliWiki Page)

RefSeq:NP_415804

PDB (EcoliWiki Page)

PDB:1DFG

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Notes

Links

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Name URL Comments
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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 1.6 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 2.7 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 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. ↑ Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  6. ↑ 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


Categories

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