O85140 (FABD_SALTY) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	STM1194

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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

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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 309

308

Malonyl CoA-acyl carrier protein transacylase

PRO_0000194219

Sites

Active site

92

1

By similarity

Active site

201

1

By similarity

Secondary structure

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309

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Helix

20 – 25

6

Helix

28 – 39

12

Helix

44 – 49

6

Helix

53 – 56

4

Helix

59 – 79

21

Helix

96 – 101

6

Helix

107 – 116

10

Helix

120 – 123

4

Beta strand

133 – 136

4

Helix

140 – 151

12

Beta strand

157 – 161

5

Beta strand

167 – 170

4

Helix

173 – 178

6

Helix

182 – 185

4

Beta strand

190 – 193

4

Helix

203 – 205

3

Helix

206 – 217

12

Beta strand

228 – 230

3

Turn

231 – 234

4

Helix

240 – 250

11

Helix

257 – 266

10

Beta strand

271 – 274

4

Helix

285 – 288

4

Beta strand

293 – 296

4

Helix

300 – 307

8

Sequences

	Sequence		Length	Mass (Da)
	O85140 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 73B4AB6EF02127DE	FASTA	309	32,405
	10 20 30 40 50 60 MTQFAFVFPG QGSQSVGMLA EMAANYPIVE ETFAEASAAL GYDLWALTQQ GPAEELNKTW 70 80 90 100 110 120 QTQPALLTAS VALWRVWQQQ GGKMPALMAG HSLGEYSALV CAGVINFADA VRLVEMRGKF 130 140 150 160 170 180 MQEAVPEGTG GMSAIIGLDD ASIAKACEES AEGQVVSPVN FNSPGQVVIA GHKEAVERAG 190 200 210 220 230 240 AACKAAGAKR ALPLPVSVPS HCALMKPAAD KLAVELAKIT FSAPTVPVVN NVDVKCETDA 250 260 270 280 290 300 AAIRDALVRQ LYNPVQWTKS VEFIAAQGVE HLYEVGPGKV LTGLTKRIVD TLTASALNEP AALSAALTQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster." Zhang Y., Cronan J.E. Jr. J. Bacteriol. 180:3295-3303(1998) [PubMed: 9642179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF044668 Genomic DNA. Translation: AAC38649.1.
AE006468 Genomic DNA. Translation: AAL20123.1.

RefSeq

NP_460164.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3H0P	X-ray	2.00	A/B	1-309	[»]

ProteinModelPortal

O85140.

SMR

O85140. Positions 3-307.

ModBase

Search...

Proteomic databases

PRIDE

O85140.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1252712.

GenomeReviews

Gene locus STM1194 in contig AE006468_GR.

KEGG

stm:STM1194.

PATRIC

32380837. VBISalEnt20916_1263.

Phylogenomic databases

HOGENOM

HBG687898.

OMA

NAMQAAV.

ProtClustDB

CLSK2459431.

Enzyme and pathway databases

BioCyc

STYP99287:STM1194-MONOMER.

Family and domain databases

InterPro

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]

Gene3D

G3DSA:3.40.366.10. Ac_transferase_reg. 2 hits.

KO

K00645.

Pfam

PF00698. Acyl_transf_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000446. Mct. 1 hit.

SUPFAM

SSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF55048. Malonyl_transacylase_ACP-bd. 1 hit.

TIGRFAMs

TIGR00128. FabD. 1 hit.

ProtoNet

Search...

Entry information

Entry name

FABD_SALTY

Accession

Primary (citable) accession number: O85140

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program