Malonyl CoA-acyl carrier protein transacylase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0AAI9 (FABD_ECOLI)

Last modified November 3, 2009. Version 40. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Malonyl CoA-acyl carrier protein transacylase
      Short name=MCT
    EC=2.3.1.39

Gene names

Name:	fabD
Synonyms:	tfpA
Ordered Locus Names:	b1092, JW1078

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].
Pathway	Lipid metabolism; fatty acid biosynthesis.
Sequence similarities	Belongs to the fabD family.

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Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	[acyl-carrier-protein] S-malonyltransferase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1 Ref.8 Ref.9

Chain

2 – 309

308

Malonyl CoA-acyl carrier protein transacylase

PRO_0000194213

Sites

Active site

201

Secondary structure

309

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AAI9-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3572E0681D14AB4A
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FASTA

309

32,417

        10         20         30         40         50         60 
MTQFAFVFPG QGSQTVGMLA DMAASYPIVE ETFAEASAAL GYDLWALTQQ GPAEELNKTW 

        70         80         90        100        110        120 
QTQPALLTAS VALYRVWQQQ GGKAPAMMAG HSLGEYSALV CAGVIDFADA VRLVEMRGKF 

       130        140        150        160        170        180 
MQEAVPEGTG AMAAIIGLDD ASIAKACEEA AEGQVVSPVN FNSPGQVVIA GHKEAVERAG 

       190        200        210        220        230        240 
AACKAAGAKR ALPLPVSVPS HCALMKPAAD KLAVELAKIT FNAPTVPVVN NVDVKCETNG 

       250        260        270        280        290        300 
DAIRDALVRQ LYNPVQWTKS VEYMAAQGVE HLYEVGPGKV LTGLTKRIVD TLTASALNEP 


SAMAAALEL

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1339356] [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: 1314802] [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: 7700236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 1556094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 289-309. Strain: K12.
[8]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB 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: 9298646] [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: 7768883] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

PIR

B41856.

RefSeq

AP_001718.1.
NP_415610.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MLA	X-ray	1.50	A	1-309	[»]
2G1H	X-ray	1.86	A	2-308	[»]
2G2O	X-ray	1.76	A	2-308	[»]
2G2Y	X-ray	2.26	A	2-308	[»]
2G2Z	X-ray	2.80	A	2-308	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0AAI9.

2-D gel databases

SWISS-2DPAGE

P0AAI9.

Genome annotation databases

GeneID

945766.

GenomeReviews

Gene locus JW1078 in contig AP009048_GR.
Gene locus b1092 in contig U00096_GR.

KEGG

ecj:JW1078.
eco:b1092.

Organism-specific databases

EchoBASE

EB1293.

EcoGene

EG11317. fabD.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AAI9.

OMA

CEIAKAK.

Enzyme and pathway databases

BioCyc

EcoCyc:MALONYL-COA-ACP-TRANSACYL-MON.
MetaCyc:MALONYL-COA-ACP-TRANSACYL-MON.

Gene expression databases

Genevestigator

P0AAI9.

Family and domain databases

InterPro

IPR014043. Acyl_transferase.
IPR004410. FabD.
[Graphical view]

Pfam

PF00698. Acyl_transf_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00128. fabD. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

FABD_ECOLI

Accession

Primary (citable) accession number: P0AAI9
Secondary accession number(s): P25715

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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