P28790 (FADA_PSEFR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-ketoacyl-CoA thiolase
EC=2.3.1.16

Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta

Gene names

Name:	fadA
Synonyms:	faoB

Organism

Pseudomonas fragi

Taxonomic identifier

296 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	391 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 final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. HAMAP MF_01620
Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.
Subcellular location	Cytoplasm By similarity HAMAP MF_01620.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fadB	P28793	3	EBI-1039311,EBI-1039318

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP MF_01620

Chain

2 – 391

390

3-ketoacyl-CoA thiolase HAMAP MF_01620

PRO_0000206380

Sites

Active site

95

1

Acyl-thioester intermediate By similarity

Active site

347

1

Proton acceptor By similarity

Active site

377

1

Proton acceptor By similarity

Secondary structure

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391

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Turn

21 – 23

3

Turn

25 – 28

4

Helix

31 – 45

15

Helix

51 – 53

3

Beta strand

54 – 60

7

Beta strand

62 – 66

5

Turn

67 – 71

5

Helix

72 – 77

6

Beta strand

80 – 82

3

Beta strand

86 – 92

7

Helix

94 – 96

3

Helix

97 – 110

14

Beta strand

115 – 124

10

Turn

125 – 127

3

Turn

130 – 133

4

Helix

138 – 142

5

Helix

146 – 149

4

Helix

151 – 162

12

Helix

166 – 185

20

Turn

186 – 192

7

Beta strand

196 – 199

4

Beta strand

205 – 208

4

Helix

220 – 224

5

Turn

232 – 234

3

Helix

239 – 241

3

Beta strand

246 – 256

11

Helix

257 – 262

6

Beta strand

268 – 278

11

Helix

281 – 286

6

Helix

288 – 299

12

Helix

303 – 305

3

Beta strand

308 – 311

4

Helix

316 – 325

10

Helix

329 – 331

3

Helix

332 – 335

4

Helix

342 – 345

4

Helix

349 – 366

18

Beta strand

370 – 378

9

Turn

379 – 381

3

Beta strand

382 – 389

8

Sequences

	Sequence		Length	Mass (Da)
	P28790 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3C5F24D816DB9EA5	FASTA	391	41,606
	10 20 30 40 50 60 MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KVLERNSKVD PGEVEDVIWG 70 80 90 100 110 120 CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TGNGDVFVVG 130 140 150 160 170 180 GVEHMGHVSM MHGVDPNPHM SLYAAKASGM MGLTAEMLGK MHGISREQQD AFAVRSHQLA 190 200 210 220 230 240 HKATVEGKFK DEIIPMQGYD ENGFLKIFDY DETIRPDTTL ESLAALKPAF NPKGGTVTAG 250 260 270 280 290 300 TSSQITDGAS CMIVMSAQRA KDLGLEPLAV IRSMAVAGVD PAIMGYGPVP ATQKALKRAG 310 320 330 340 350 360 LNMADIDFIE LNEAFAAQAL PVLKDLKVLD KMNEKVNLHG GAIALGHPFG CSGARISGTL 370 380 390 LNVMKQNGGT FGLSTMCIGL GQGIATVFER V

References

[1]	"Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation." Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A. J. Biochem. 111:8-15(1992) [PubMed: 1607366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: B-0771.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D10390 Genomic DNA. Translation: BAA01228.1.

PIR

JS0624.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WDK	X-ray	2.50	C/D	2-390	[»]
1WDL	X-ray	3.50	C/D	2-390	[»]
1WDM	X-ray	3.80	C/D	2-390	[»]
2D3T	X-ray	3.40	C/D	2-390	[»]

ProteinModelPortal

P28790.

SMR

P28790. Positions 2-391.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29090N.

IntAct

P28790. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_01620. FadA.
[Tree]

InterPro

IPR012805. FadA.
IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]

Gene3D

G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.

PANTHER

PTHR18919:SF35. PTHR18919:SF35. 1 hit.
PTHR18919. Thiolase. 1 hit.

Pfam

PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000429. Ac-CoA_Ac_transf. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

TIGRFAMs

TIGR01930. AcCoA-C-Actrans. 1 hit.
TIGR02445. FadA. 1 hit.

PROSITE

PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FADA_PSEFR

Accession

Primary (citable) accession number: P28790

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program