P0AAI5 (FABF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 2
EC=2.3.1.179

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase II
Beta-ketoacyl-ACP synthase II
Short name=KAS II

Gene names

Name:	fabF
Synonyms:	fabJ
Ordered Locus Names:	b1095, JW1081

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	413 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)

Function	Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
Catalytic activity	(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the beta-ketoacyl-ACP synthases family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from direct assay PubMed 237914. Source: EcoCyc beta-ketoacyl-acyl-carrier-protein synthase II activity Inferred from direct assay PubMed 7002930. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	2	EBI-542783,EBI-542092

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 413

412

3-oxoacyl-[acyl-carrier-protein] synthase 2

PRO_0000180314

Sites

Active site

164

1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

413

Helix Strand Turn

Details...

Beta strand

6 – 15

10

Beta strand

18 – 20

3

Helix

21 – 29

9

Beta strand

35 – 37

3

Beta strand

50 – 52

3

Turn

60 – 62

3

Helix

65 – 68

4

Helix

73 – 89

17

Turn

95 – 97

3

Helix

98 – 100

3

Beta strand

101 – 106

6

Helix

112 – 125

14

Helix

127 – 129

3

Helix

134 – 138

5

Helix

142 – 151

10

Helix

163 – 165

3

Helix

166 – 180

15

Beta strand

184 – 192

9

Helix

197 – 205

9

Helix

216 – 219

4

Beta strand

235 – 243

9

Helix

244 – 249

6

Beta strand

256 – 265

10

Beta strand

270 – 272

3

Helix

278 – 291

14

Helix

295 – 297

3

Beta strand

300 – 302

3

Helix

309 – 323

15

Helix

324 – 328

5

Beta strand

330 – 333

4

Helix

336 – 339

4

Helix

343 – 345

3

Helix

346 – 360

15

Beta strand

370 – 372

3

Beta strand

382 – 384

3

Beta strand

393 – 400

8

Turn

401 – 403

3

Beta strand

404 – 411

8

Sequences

	Sequence		Length	Mass (Da)
	P0AAI5 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5F60DB1F986B2EE5	FASTA	413	43,046
	10 20 30 40 50 60 MSKRRVVVTG LGMLSPVGNT VESTWKALLA GQSGISLIDH FDTSAYATKF AGLVKDFNCE 70 80 90 100 110 120 DIISRKEQRK MDAFIQYGIV AGVQAMQDSG LEITEENATR IGAAIGSGIG GLGLIEENHT 130 140 150 160 170 180 SLMNGGPRKI SPFFVPSTIV NMVAGHLTIM YGLRGPSISI ATACTSGVHN IGHAARIIAY 190 200 210 220 230 240 GDADVMVAGG AEKASTPLGV GGFGAARALS TRNDNPQAAS RPWDKERDGF VLGDGAGMLV 250 260 270 280 290 300 LEEYEHAKKR GAKIYAELVG FGMSSDAYHM TSPPENGAGA ALAMANALRD AGIEASQIGY 310 320 330 340 350 360 VNAHGTSTPA GDKAEAQAVK TIFGEAASRV LVSSTKSMTG HLLGAAGAVE SIYSILALRD 370 380 390 400 410 QAVPPTINLD NPDEGCDLDF VPHEARQVSG MEYTLCNSFG FGGTNGSLIF KKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates." Siggaard-Andersen M., Wissenbach M., Chuck J.-A., Svendsen I., Olsen J.G., von Wettstein-Knowles P.V. Proc. Natl. Acad. Sci. U.S.A. 91:11027-11031(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-32. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene." Magnuson K., Carey M.R., Cronan J.E. Jr. J. Bacteriol. 177:3593-3595(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTITY OF FABF AND FABJ. Strain: K12 / UB1005.
[3]	"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. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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.
[6]	"Altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants." Jackowski S., Rock C.O. J. Bacteriol. 169:1469-1473(1987) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF FABF AS KASII.
[7]	"Beta-ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis." Garwin J.L., Klages A.L., Cronan J.E. Jr. J. Biol. Chem. 255:3263-3265(1980) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes from Escherichia coli." Edwards P., Nelsen J.S., Metz J.G., Dehesh K. FEBS Lett. 402:62-66(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes." Huang W., Jia J., Edwards P., Dehesh K., Schneider G., Lindqvist Y. EMBO J. 17:1183-1191(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[10]	"Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase." Moche M., Schneider G., Edwards P., Dehesh K., Lindqvist Y. J. Biol. Chem. 274:6031-6034(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z34979 Genomic DNA. Translation: CAA84431.1.
U20767 Genomic DNA. Translation: AAA83255.1.
U00096 Genomic DNA. Translation: AAC74179.1.
AP009048 Genomic DNA. Translation: BAA35903.1.

PIR

I41060.

RefSeq

NP_415613.1. NC_000913.2.
YP_489363.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B3N	X-ray	2.65	A	2-413	[»]
1KAS	X-ray	2.40	A	2-413	[»]
2GFV	X-ray	2.29	A	2-412	[»]
2GFW	X-ray	2.40	A	2-412	[»]
2GFX	X-ray	2.59	A	2-412	[»]
2GFY	X-ray	2.85	A	2-412	[»]
3G0Y	X-ray	2.60	A	2-413	[»]
3G11	X-ray	2.00	A	2-413	[»]
3HNZ	X-ray	2.75	A	2-413	[»]
3HO2	X-ray	2.00	A	2-413	[»]
3HO9	X-ray	1.90	A	2-413	[»]
3I8P	X-ray	1.90	A	2-413	[»]

ProteinModelPortal

P0AAI5.

SMR

P0AAI5. Positions 3-413.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29377N.

IntAct

P0AAI5. 6 interactions.

MINT

MINT-1231688.

STRING

511145.b1095.

Proteomic databases

PaxDb

P0AAI5.

PRIDE

P0AAI5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74179; AAC74179; b1095.
BAA35903; BAA35903; BAA35903.

GeneID

12931078.
946665.

KEGG

ecj:Y75_p1065.
eco:b1095.

PATRIC

32117431. VBIEscCol129921_1138.

Organism-specific databases

EchoBASE

EB2490.

EcoGene

EG12606. fabF.

Phylogenomic databases

eggNOG

COG0304.

HOGENOM

HOG000060165.

KO

K09458.

OMA

INMISGF.

ProtClustDB

PRK07314.

Enzyme and pathway databases

BioCyc

EcoCyc:3-OXOACYL-ACP-SYNTHII-MONOMER.
ECOL316407:JW1081-MONOMER.
MetaCyc:3-OXOACYL-ACP-SYNTHII-MONOMER.

BRENDA

2.3.1.179. 2026.

SABIO-RK

P0AAI5.

UniPathway

UPA00094.

Gene expression databases

Genevestigator

P0AAI5.

Family and domain databases

Gene3D

3.40.47.10. 2 hits.

InterPro

IPR017568. 3-oxoacyl-ACP_synth-2.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Pfam

PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000447. KAS_II. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

TIGRFAMs

TIGR03150. fabF. 1 hit.

PROSITE

PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01034. Cerulenin.

EvolutionaryTrace

P0AAI5.

Entry information

Entry name

FABF_ECOLI

Accession

Primary (citable) accession number: P0AAI5
Secondary accession number(s): P39435

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program