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P0AAI9

- FABD_ECOLI

UniProt

P0AAI9 - FABD_ECOLI

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Protein

Malonyl CoA-acyl carrier protein transacylase

Gene

fabD

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 transacylasePRO_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

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Turni16 – 194Combined sources
Helixi20 – 256Combined sources
Helixi28 – 4013Combined sources
Helixi44 – 507Combined sources
Helixi53 – 564Combined sources
Helixi59 – 7921Combined sources
Beta strandi86 – 916Combined sources
Helixi93 – 1019Combined sources
Helixi107 – 12418Combined sources
Beta strandi129 – 1379Combined sources
Helixi140 – 15011Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi166 – 1727Combined sources
Helixi173 – 18513Combined sources
Beta strandi189 – 1935Combined sources
Helixi203 – 2053Combined sources
Helixi206 – 21712Combined sources
Turni231 – 2333Combined sources
Helixi240 – 25213Combined sources
Helixi257 – 26610Combined sources
Beta strandi271 – 2744Combined sources
Beta strandi276 – 2794Combined sources
Helixi280 – 2889Combined sources
Beta strandi293 – 2964Combined sources
Helixi300 – 3067Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
SMRiP0AAI9. Positions 3-307.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AAI9.

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.Curated

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000036503.
InParanoidiP0AAI9.
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

        10         20         30         40         50
MTQFAFVFPG QGSQTVGMLA DMAASYPIVE ETFAEASAAL GYDLWALTQQ
60 70 80 90 100
GPAEELNKTW QTQPALLTAS VALYRVWQQQ GGKAPAMMAG HSLGEYSALV
110 120 130 140 150
CAGVIDFADA VRLVEMRGKF MQEAVPEGTG AMAAIIGLDD ASIAKACEEA
160 170 180 190 200
AEGQVVSPVN FNSPGQVVIA GHKEAVERAG AACKAAGAKR ALPLPVSVPS
210 220 230 240 250
HCALMKPAAD KLAVELAKIT FNAPTVPVVN NVDVKCETNG DAIRDALVRQ
260 270 280 290 300
LYNPVQWTKS VEYMAAQGVE HLYEVGPGKV LTGLTKRIVD TLTASALNEP

SAMAAALEL
Length:309
Mass (Da):32,417
Last modified:January 23, 2007 - v2
Checksum:i3572E0681D14AB4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
SMRi P0AAI9. Positions 3-307.
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.
InParanoidi P0AAI9.
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: November 26, 2014
This is version 85 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