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P0AAI9

- FABD_ECOLI

UniProt

P0AAI9 - FABD_ECOLI

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Protein
Malonyl CoA-acyl carrier protein transacylase
Gene
fabD, tfpA, b1092, JW1078
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921
Active sitei201 – 2011

GO - Molecular functioni

  1. [acyl-carrier-protein] S-malonyltransferase activity Source: EcoCyc

GO - Biological processi

  1. fatty acid biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:MALONYL-COA-ACP-TRANSACYL-MONOMER.
ECOL316407:JW1078-MONOMER.
MetaCyc:MALONYL-COA-ACP-TRANSACYL-MONOMER.
RETL1328306-WGS:GSTH-1455-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl CoA-acyl carrier protein transacylase (EC:2.3.1.39)
Short name:
MCT
Gene namesi
Name:fabD
Synonyms:tfpA
Ordered Locus Names:b1092, JW1078
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11317. fabD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 309308Malonyl CoA-acyl carrier protein transacylase
PRO_0000194213Add
BLAST

Proteomic databases

PaxDbiP0AAI9.
PRIDEiP0AAI9.

2D gel databases

SWISS-2DPAGEP0AAI9.

Expressioni

Gene expression databases

GenevestigatoriP0AAI9.

Interactioni

Protein-protein interaction databases

DIPiDIP-47923N.
IntActiP0AAI9. 4 interactions.
STRINGi511145.b1092.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Turni16 – 194
Helixi20 – 256
Helixi28 – 4013
Helixi44 – 507
Helixi53 – 564
Helixi59 – 7921
Beta strandi86 – 916
Helixi93 – 1019
Helixi107 – 12418
Beta strandi129 – 1379
Helixi140 – 15011
Beta strandi156 – 1638
Beta strandi166 – 1727
Helixi173 – 18513
Beta strandi189 – 1935
Helixi203 – 2053
Helixi206 – 21712
Turni231 – 2333
Helixi240 – 25213
Helixi257 – 26610
Beta strandi271 – 2744
Beta strandi276 – 2794
Helixi280 – 2889
Beta strandi293 – 2964
Helixi300 – 3067

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MLAX-ray1.50A1-309[»]
2G1HX-ray1.86A2-309[»]
2G2OX-ray1.76A2-309[»]
2G2YX-ray2.26A2-309[»]
2G2ZX-ray2.80A2-309[»]
ProteinModelPortaliP0AAI9.

Miscellaneous databases

EvolutionaryTraceiP0AAI9.

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036503.
KOiK00645.
OMAiIWRVWQE.
OrthoDBiEOG6W19KW.
PhylomeDBiP0AAI9.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AAI9-1 [UniParc]FASTAAdd to Basket

« Hide

MTQFAFVFPG QGSQTVGMLA DMAASYPIVE ETFAEASAAL GYDLWALTQQ    50
GPAEELNKTW QTQPALLTAS VALYRVWQQQ GGKAPAMMAG HSLGEYSALV 100
CAGVIDFADA VRLVEMRGKF MQEAVPEGTG AMAAIIGLDD ASIAKACEEA 150
AEGQVVSPVN FNSPGQVVIA GHKEAVERAG AACKAAGAKR ALPLPVSVPS 200
HCALMKPAAD KLAVELAKIT FNAPTVPVVN NVDVKCETNG DAIRDALVRQ 250
LYNPVQWTKS VEYMAAQGVE HLYEVGPGKV LTGLTKRIVD TLTASALNEP 300
SAMAAALEL 309
Length:309
Mass (Da):32,417
Last modified:January 23, 2007 - v2
Checksum:i3572E0681D14AB4A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87040 Genomic DNA. Translation: AAA23742.1.
Z11565 Genomic DNA. Translation: CAA77658.1.
U00096 Genomic DNA. Translation: AAC74176.1.
AP009048 Genomic DNA. Translation: BAA35900.1.
M84991 Genomic DNA. Translation: AAA23738.1.
PIRiB41856.
RefSeqiNP_415610.1. NC_000913.3.
YP_489360.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74176; AAC74176; b1092.
BAA35900; BAA35900; BAA35900.
GeneIDi12934374.
945766.
KEGGiecj:Y75_p1062.
eco:b1092.
PATRICi32117425. VBIEscCol129921_1135.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87040 Genomic DNA. Translation: AAA23742.1 .
Z11565 Genomic DNA. Translation: CAA77658.1 .
U00096 Genomic DNA. Translation: AAC74176.1 .
AP009048 Genomic DNA. Translation: BAA35900.1 .
M84991 Genomic DNA. Translation: AAA23738.1 .
PIRi B41856.
RefSeqi NP_415610.1. NC_000913.3.
YP_489360.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MLA X-ray 1.50 A 1-309 [» ]
2G1H X-ray 1.86 A 2-309 [» ]
2G2O X-ray 1.76 A 2-309 [» ]
2G2Y X-ray 2.26 A 2-309 [» ]
2G2Z X-ray 2.80 A 2-309 [» ]
ProteinModelPortali P0AAI9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47923N.
IntActi P0AAI9. 4 interactions.
STRINGi 511145.b1092.

2D gel databases

SWISS-2DPAGE P0AAI9.

Proteomic databases

PaxDbi P0AAI9.
PRIDEi P0AAI9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74176 ; AAC74176 ; b1092 .
BAA35900 ; BAA35900 ; BAA35900 .
GeneIDi 12934374.
945766.
KEGGi ecj:Y75_p1062.
eco:b1092.
PATRICi 32117425. VBIEscCol129921_1135.

Organism-specific databases

EchoBASEi EB1293.
EcoGenei EG11317. fabD.

Phylogenomic databases

eggNOGi COG0331.
HOGENOMi HOG000036503.
KOi K00645.
OMAi IWRVWQE.
OrthoDBi EOG6W19KW.
PhylomeDBi P0AAI9.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci EcoCyc:MALONYL-COA-ACP-TRANSACYL-MONOMER.
ECOL316407:JW1078-MONOMER.
MetaCyc:MALONYL-COA-ACP-TRANSACYL-MONOMER.
RETL1328306-WGS:GSTH-1455-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AAI9.
PROi P0AAI9.

Gene expression databases

Genevestigatori P0AAI9.

Family and domain databases

Gene3Di 3.40.366.10. 2 hits.
InterProi IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000446. Mct. 1 hit.
SUPFAMi SSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsi TIGR00128. fabD. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli."
    Magnuson K., Oh W., Larson T.J., Cronan J.E. Jr.
    FEBS Lett. 299:262-266(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
    Strain: K12.
  2. "Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase."
    Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J., Stuitje A.R.
    J. Bacteriol. 174:2851-2857(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Resistance to trifluoroperazine, a calmodulin inhibitor, maps to the fabD locus in Escherichia coli."
    Bouquin N., Tempete M., Holland I.B., Seror S.J.
    Mol. Gen. Genet. 246:628-637(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes."
    Rawlings M., Cronan J.E. Jr.
    J. Biol. Chem. 267:5751-5754(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 289-309.
    Strain: K12.
  8. Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: K12 / EMG2.
  10. "The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component."
    Serre L., Verbree E.C., Dauter Z., Stuitje A.R., Derewenda Z.S.
    J. Biol. Chem. 270:12961-12964(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Entry informationi

Entry nameiFABD_ECOLI
AccessioniPrimary (citable) accession number: P0AAI9
Secondary accession number(s): P25715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi