P0A953 (FABB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 1
EC=2.3.1.41

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

Gene names

Name:	fabB
Synonyms:	fabC
Ordered Locus Names:	b2323, JW2320

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	406 AA.
Sequence status	Complete.
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. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids. Ref.6
Catalytic activity	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the beta-ketoacyl-ACP synthases family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
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 genetic interaction PubMed 19679654. Source: EcoliWiki
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 406

406

3-oxoacyl-[acyl-carrier-protein] synthase 1

PRO_0000180311

Sites

Active site

163

1

Natural variations

Natural variant

4

1

A → T in strain: MA-1 / fabB3.

Natural variant

140

1

S → F in strain: K1060 / fabB5.

Natural variant

299

1

G → S in strain: MA-1 / fabB3.

Natural variant

329

1

A → V in strain: M5 / fabB15.

Secondary structure

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406

Helix Strand Turn

Details...

Beta strand

4 – 13

10

Beta strand

16 – 18

3

Helix

19 – 28

10

Beta strand

33 – 35

3

Helix

37 – 41

5

Beta strand

48 – 50

3

Turn

57 – 59

3

Helix

62 – 65

4

Helix

70 – 86

17

Helix

90 – 93

4

Beta strand

99 – 104

6

Beta strand

106 – 108

3

Helix

110 – 120

11

Turn

123 – 125

3

Helix

126 – 129

4

Helix

133 – 137

5

Helix

141 – 147

7

Turn

148 – 151

4

Beta strand

156 – 160

5

Helix

162 – 164

3

Helix

165 – 178

14

Beta strand

183 – 191

9

Helix

195 – 203

9

Turn

211 – 213

3

Helix

215 – 217

3

Beta strand

234 – 242

9

Helix

243 – 248

6

Beta strand

255 – 264

10

Beta strand

269 – 271

3

Helix

275 – 285

11

Beta strand

294 – 296

3

Helix

303 – 317

15

Helix

318 – 320

3

Beta strand

323 – 325

3

Helix

328 – 331

4

Helix

335 – 337

3

Helix

338 – 352

15

Beta strand

362 – 364

3

Helix

366 – 368

3

Beta strand

371 – 373

3

Beta strand

384 – 391

8

Turn

392 – 394

3

Beta strand

395 – 402

8

Sequences

	Sequence		Length	Mass (Da)
	P0A953 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 489D8BAD23E78113	FASTA	406	42,613
	10 20 30 40 50 60 MKRAVITGLG IVSSIGNNQQ EVLASLREGR SGITFSQELK DSGMRSHVWG NVKLDTTGLI 70 80 90 100 110 120 DRKVVRFMSD ASIYAFLSME QAIADAGLSP EAYQNNPRVG LIAGSGGGSP RFQVFGADAM 130 140 150 160 170 180 RGPRGLKAVG PYVVTKAMAS GVSACLATPF KIHGVNYSIS SACATSAHCI GNAVEQIQLG 190 200 210 220 230 240 KQDIVFAGGG EELCWEMACE FDAMGALSTK YNDTPEKASR TYDAHRDGFV IAGGGGMVVV 250 260 270 280 290 300 EELEHALARG AHIYAEIVGY GATSDGADMV APSGEGAVRC MKMAMHGVDT PIDYLNSHGT 310 320 330 340 350 360 STPVGDVKEL AAIREVFGDK SPAISATKAM TGHSLGAAGV QEAIYSLLML EHGFIAPSIN 370 380 390 400 IEELDEQAAG LNIVTETTDR ELTTVMSNSF GFGGTNATLV MRKLKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Beta-ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue." Kauppinen S., Siggaard-Andersen M., von Wettstein-Knowles P. Carlsberg Res. Commun. 53:357-370(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 158-168. Strain: B.
[2]	"Catalytic residues of beta-ketoacyl-ACP synthases." Siggaard-Andersen M., von Wettstein-Knowles P., Gotthardt-Olsen J., Bangera G., Chuck J.-A., Pontoppidan B. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K1060 / fabB5, M5 / fabB15 and MA-1 / fabB3.
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [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]	"Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis." Siggaard-Andersen M. Carlsberg Res. Commun. 53:371-379(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN UNSATURATED FATTY ACID SYNTHESIS.
[7]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[8]	"The X-ray crystal structure of beta-ketoacyl [acyl carrier-protein] synthase I." Olsen J.G., Kadziola A., von Wettstein-Knowles P., Siggaard-Andersen M., Lindquist Y., Larsen S. FEBS Lett. 460:46-52(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M24427 Genomic DNA. Translation: AAC67304.1.
AJ012161 Genomic DNA. Translation: CAA09932.1.
AJ012162 Genomic DNA. Translation: CAA09933.1.
AJ012163 Genomic DNA. Translation: CAA09934.1.
U00096 Genomic DNA. Translation: AAC75383.1.
AP009048 Genomic DNA. Translation: BAA16180.1.

PIR

SYECA1. A31284.

RefSeq

NP_416826.1. NC_000913.2.
YP_490565.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DD8	X-ray	2.30	A/B/C/D	1-406	[»]
1EK4	X-ray	1.85	A/B/C/D	1-406	[»]
1F91	X-ray	2.40	A/B/C/D	1-406	[»]
1FJ4	X-ray	2.35	A/B/C/D	1-406	[»]
1FJ8	X-ray	2.27	A/B/C/D	1-406	[»]
1G5X	X-ray	2.45	A/B/C/D	1-406	[»]
1H4F	X-ray	2.00	A/B/C/D	1-406	[»]
2AQ7	X-ray	2.30	A/B/C/D	1-406	[»]
2AQB	X-ray	2.19	A/B/C/D	1-406	[»]
2BUH	X-ray	1.90	A/B/C/D	1-406	[»]
2BUI	X-ray	2.40	A/B/C/D	1-406	[»]
2BYW	X-ray	1.70	A/B/C/D	1-406	[»]
2BYX	X-ray	2.00	A/B/C/D	1-406	[»]
2BYY	X-ray	2.20	A/B/C/D	1-406	[»]
2BYZ	X-ray	1.95	A/B/C/D	1-406	[»]
2BZ3	X-ray	2.00	A/B/C/D	1-406	[»]
2BZ4	X-ray	1.86	A/B/C/D	1-406	[»]
2VB7	X-ray	1.60	A/B/C/D	1-406	[»]
2VB8	X-ray	1.52	A/B/C/D	1-406	[»]
2VB9	X-ray	1.50	A/B/C/D	1-406	[»]
2VBA	X-ray	1.36	A/B/C/D	1-406	[»]

ProteinModelPortal

P0A953.

SMR

P0A953. Positions 1-406.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29379N.

IntAct

P0A953. 9 interactions.

MINT

MINT-1235843.

STRING

511145.b2323.

Proteomic databases

PaxDb

P0A953.

PRIDE

P0A953.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75383; AAC75383; b2323.
BAA16180; BAA16180; BAA16180.

GeneID

12931799.
946799.

KEGG

ecj:Y75_p2289.
eco:b2323.

PATRIC

32120019. VBIEscCol129921_2419.

Organism-specific databases

EchoBASE

EB0270.

EcoGene

EG10274. fabB.

Phylogenomic databases

eggNOG

COG0304.

HOGENOM

HOG000060165.

KO

K00647.

OMA

FAGGHED.

ProtClustDB

PRK07967.

Enzyme and pathway databases

BioCyc

EcoCyc:FABB-MONOMER.
ECOL316407:JW2320-MONOMER.
MetaCyc:FABB-MONOMER.

UniPathway

UPA00094.

Gene expression databases

Genevestigator

P0A953.

Family and domain databases

Gene3D

3.40.47.10. 2 hits.

InterPro

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]

SUPFAM

SSF53901. Thiolase-like. 2 hits.

PROSITE

PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P0A953.

ChEMBL

CHEMBL4913.

DrugBank

DB01034. Cerulenin.

EvolutionaryTrace

P0A953.

Entry information

Entry name

FABB_ECOLI

Accession

Primary (citable) accession number: P0A953
Secondary accession number(s): P14926 , Q9R828, Q9R829, Q9R830

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program